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Multifunctional-autoprocessing repeats-in-toxin (MARTX) (EC 3.4.22.-) [Cleaved into: Actin cross-linking toxin F1 (EC 6.3.2.-); Actin cross-linking toxin F4 (EC 6.3.2.-); Rho inactivation domain-containing toxin F2; ABH effector region toxin F5; Cysteine protease domain-containing toxin F3 (EC 3.4.22.-)]

 MARTX_VIBCH             Reviewed;        4558 AA.
Q9KS12; Q9X4W2;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
14-OCT-2015, sequence version 2.
30-AUG-2017, entry version 111.
RecName: Full=Multifunctional-autoprocessing repeats-in-toxin {ECO:0000303|PubMed:26185092};
Short=MARTX {ECO:0000303|PubMed:26185092};
EC=3.4.22.- {ECO:0000269|PubMed:17464284};
Contains:
RecName: Full=Actin cross-linking toxin F1 {ECO:0000305|PubMed:19620709};
EC=6.3.2.- {ECO:0000269|PubMed:23029200};
Contains:
RecName: Full=Actin cross-linking toxin F4 {ECO:0000305|PubMed:19620709};
EC=6.3.2.- {ECO:0000269|PubMed:23029200};
Contains:
RecName: Full=Rho inactivation domain-containing toxin F2 {ECO:0000305|PubMed:19620709};
Contains:
RecName: Full=ABH effector region toxin F5 {ECO:0000305|PubMed:19620709};
Contains:
RecName: Full=Cysteine protease domain-containing toxin F3 {ECO:0000305|PubMed:19620709};
EC=3.4.22.- {ECO:0000269|PubMed:17464284};
Flags: Precursor;
Name=rtxA {ECO:0000303|PubMed:11032799};
Synonyms=rtx {ECO:0000303|PubMed:9927695};
OrderedLocusNames=VC_1451 {ECO:0000312|EMBL:AAF94608.1};
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Vibrio.
NCBI_TaxID=243277;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 39315 / El Tor Inaba N16961;
PubMed=9927695; DOI=10.1073/pnas.96.3.1071;
Lin W., Fullner K.J., Clayton R., Sexton J.A., Rogers M.B.,
Calia K.E., Calderwood S.B., Fraser C., Mekalanos J.J.;
"Identification of a vibrio cholerae RTX toxin gene cluster that is
tightly linked to the cholera toxin prophage.";
Proc. Natl. Acad. Sci. U.S.A. 96:1071-1076(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 39315 / El Tor Inaba N16961
{ECO:0000312|Proteomes:UP000000584};
PubMed=10952301; DOI=10.1038/35020000;
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
Mekalanos J.J., Venter J.C., Fraser C.M.;
"DNA sequence of both chromosomes of the cholera pathogen Vibrio
cholerae.";
Nature 406:477-483(2000).
[3]
FUNCTION (ACTIN CROSS-LINKING TOXIN F1 AND ACTIN CROSS-LINKING TOXIN
F4), AND SUBCELLULAR LOCATION.
PubMed=11032799; DOI=10.1093/emboj/19.20.5315;
Fullner K.J., Mekalanos J.J.;
"In vivo covalent cross-linking of cellular actin by the Vibrio
cholerae RTX toxin.";
EMBO J. 19:5315-5323(2000).
[4]
FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN).
PubMed=11553575; DOI=10.1128/IAI.69.10.6310-6317.2001;
Fullner K.J., Lencer W.I., Mekalanos J.J.;
"Vibrio cholerae-induced cellular responses of polarized T84
intestinal epithelial cells are dependent on production of cholera
toxin and the RTX toxin.";
Infect. Immun. 69:6310-6317(2001).
[5]
FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN).
PubMed=12045243; DOI=10.1084/jem.20020318;
Fullner K.J., Boucher J.C., Hanes M.A., Haines G.K. III, Meehan B.M.,
Walchle C., Sansonetti P.J., Mekalanos J.J.;
"The contribution of accessory toxins of Vibrio cholerae O1 El Tor to
the proinflammatory response in a murine pulmonary cholera model.";
J. Exp. Med. 195:1455-1462(2002).
[6]
SUBCELLULAR LOCATION (MULTIFUNCTIONAL-AUTOPROCESSING
REPEATS-IN-TOXIN).
PubMed=15547287; DOI=10.1128/JB.186.23.8137-8143.2004;
Boardman B.K., Satchell K.J.;
"Vibrio cholerae strains with mutations in an atypical type I
secretion system accumulate RTX toxin intracellularly.";
J. Bacteriol. 186:8137-8143(2004).
[7]
FUNCTION (ACTIN CROSS-LINKING TOXIN F1 AND ACTIN CROSS-LINKING TOXIN
F4).
PubMed=15199181; DOI=10.1073/pnas.0401104101;
Sheahan K.L., Cordero C.L., Satchell K.J.;
"Identification of a domain within the multifunctional Vibrio cholerae
RTX toxin that covalently cross-links actin.";
Proc. Natl. Acad. Sci. U.S.A. 101:9798-9803(2004).
[8]
FUNCTION (ACTIN CROSS-LINKING TOXIN F1 AND ACTIN CROSS-LINKING TOXIN
F4), AND COFACTOR.
PubMed=16954226; DOI=10.1074/jbc.M605275200;
Cordero C.L., Kudryashov D.S., Reisler E., Satchell K.J.;
"The Actin cross-linking domain of the Vibrio cholerae RTX toxin
directly catalyzes the covalent cross-linking of actin.";
J. Biol. Chem. 281:32366-32374(2006).
[9]
FUNCTION (RHO INACTIVATION DOMAIN-CONTAINING TOXIN F2).
PubMed=17474905; DOI=10.1111/j.1462-5822.2006.00876.x;
Sheahan K.L., Satchell K.J.;
"Inactivation of small Rho GTPases by the multifunctional RTX toxin
from Vibrio cholerae.";
Cell. Microbiol. 9:1324-1335(2007).
[10]
FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN), ACTIVE
SITE, CLEAVAGE SITE, ENZYME REGULATION, AND MUTAGENESIS OF HIS-3532;
GLU-3551 AND CYS-3581.
PubMed=17464284; DOI=10.1038/sj.emboj.7601700;
Sheahan K.L., Cordero C.L., Satchell K.J.;
"Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine
protease domain.";
EMBO J. 26:2552-2561(2007).
[11]
FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN AND CYSTEINE
PROTEASE DOMAIN-CONTAINING TOXIN F3).
PubMed=17698573; DOI=10.1128/IAI.00506-07;
Olivier V., Haines G.K. III, Tan Y., Satchell K.J.;
"Hemolysin and the multifunctional autoprocessing RTX toxin are
virulence factors during intestinal infection of mice with Vibrio
cholerae El Tor O1 strains.";
Infect. Immun. 75:5035-5042(2007).
[12]
FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN AND CYSTEINE
PROTEASE DOMAIN-CONTAINING TOXIN F3).
PubMed=17698571; DOI=10.1128/IAI.00508-07;
Olivier V., Salzman N.H., Satchell K.J.;
"Prolonged colonization of mice by Vibrio cholerae El Tor O1 depends
on accessory toxins.";
Infect. Immun. 75:5043-5051(2007).
[13]
FUNCTION (ACTIN CROSS-LINKING TOXIN F1 AND ACTIN CROSS-LINKING TOXIN
F4).
PubMed=17951576; DOI=10.1074/jbc.M703910200;
Kudryashov D.S., Cordero C.L., Reisler E., Satchell K.J.;
"Characterization of the enzymatic activity of the actin cross-linking
domain from the Vibrio cholerae MARTX Vc toxin.";
J. Biol. Chem. 283:445-452(2008).
[14]
FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN), ENZYME
REGULATION, CLEAVAGE SITE, AND MUTAGENESIS OF PRO-3462; ARG-3470;
ILE-3476; GLN-3478; GLU-3480; ASP-3482; ALA-3488; LEU-3492; LYS-3495;
3499-SER-SER-3500; LYS-3524; ARG-3526; HIS-3532; ARG-3534; SER-3537;
LEU-3552; LYS-3572; CYS-3581; ARG-3606; VAL-3609; ARG-3612; ARG-3623;
LYS-3624 AND LYS-3641.
PubMed=18591243; DOI=10.1074/jbc.M803334200;
Prochazkova K., Satchell K.J.;
"Structure-function analysis of inositol hexakisphosphate-induced
autoprocessing of the Vibrio cholerae multifunctional autoprocessing
RTX toxin.";
J. Biol. Chem. 283:23656-23664(2008).
[15]
FUNCTION (ACTIN CROSS-LINKING TOXIN F1 AND ACTIN CROSS-LINKING TOXIN
F4).
PubMed=19015515; DOI=10.1073/pnas.0808082105;
Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I.,
Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J.,
Reisler E.;
"Connecting actin monomers by iso-peptide bond is a toxicity mechanism
of the Vibrio cholerae MARTX toxin.";
Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008).
[16]
FUNCTION (ACTIN CROSS-LINKING TOXIN F1 AND ACTIN CROSS-LINKING TOXIN
F4), AND MUTAGENESIS OF GLU-2003; GLU-2005; LEU-2035; ASP-2038;
GLY-2055; GLU-2065; THR-2068; LEU-2089; HIS-2096; LEU-2117; GLN-2149;
ALA-2153; TRP-2175; LEU-2206; VAL-2209; TRP-2250; VAL-2259; GLU-2326
AND ARG-2328.
PubMed=19656298; DOI=10.1111/j.1365-2958.2009.06810.x;
Geissler B., Bonebrake A., Sheahan K.L., Walker M.E., Satchell K.J.;
"Genetic determination of essential residues of the Vibrio cholerae
actin cross-linking domain reveals functional similarity with
glutamine synthetases.";
Mol. Microbiol. 73:858-868(2009).
[17]
FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN).
PubMed=19812690; DOI=10.1371/journal.pone.0007352;
Olivier V., Queen J., Satchell K.J.;
"Successful small intestine colonization of adult mice by Vibrio
cholerae requires ketamine anesthesia and accessory toxins.";
PLoS ONE 4:E7352-E7352(2009).
[18]
FUNCTION (RHO INACTIVATION DOMAIN-CONTAINING TOXIN F2).
PubMed=19434753; DOI=10.1002/prot.22447;
Pei J., Grishin N.V.;
"The Rho GTPase inactivation domain in Vibrio cholerae MARTX toxin has
a circularly permuted papain-like thiol protease fold.";
Proteins 77:413-419(2009).
[19]
SUBCELLULAR LOCATION (RHO INACTIVATION DOMAIN-CONTAINING TOXIN F2),
AND MUTAGENESIS OF TYR-2596; SER-2641 AND ARG-2643.
PubMed=20212166; DOI=10.1073/pnas.0908700107;
Geissler B., Tungekar R., Satchell K.J.;
"Identification of a conserved membrane localization domain within
numerous large bacterial protein toxins.";
Proc. Natl. Acad. Sci. U.S.A. 107:5581-5586(2010).
[20]
SUBCELLULAR LOCATION (RHO INACTIVATION DOMAIN-CONTAINING TOXIN F2).
PubMed=22044757; DOI=10.1111/j.1462-5822.2011.01718.x;
Geissler B., Ahrens S., Satchell K.J.;
"Plasma membrane association of three classes of bacterial toxins is
mediated by a basic-hydrophobic motif.";
Cell. Microbiol. 14:286-298(2012).
[21]
FUNCTION (ACTIN CROSS-LINKING TOXIN F1 AND ACTIN CROSS-LINKING TOXIN
F4), BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=23029200; DOI=10.1371/journal.pone.0045721;
Kudryashova E., Kalda C., Kudryashov D.S.;
"Glutamyl phosphate is an activated intermediate in actin crosslinking
by actin crosslinking domain (ACD) toxin.";
PLoS ONE 7:E45721-E45721(2012).
[22]
FUNCTION (RHO INACTIVATION DOMAIN-CONTAINING TOXIN F2), AND
MUTAGENESIS OF GLU-2734; TYR-2735; ASP-2760; LEU-2764; LYS-2766;
HIS-2768; GLU-2772; SER-2776; SER-2779; THR-2781; LYS-2786; SER-2788;
HIS-2790; SER-2791; LEU-2793; HIS-2795; LEU-2798; ARG-2804; TYR-2820;
SER-2822; LYS-2829; SER-2830; ARG-2850; LEU-2864; ASP-2867; GLU-2871;
GLU-2872; ASP-2874; ARG-2887; LEU-2914; ARG-2950; ARG-2956; ARG-2961;
ARG-2971; ARG-2977; GLU-2981; ARG-2982; LYS-2991; SER-2993; ASP-2996;
ARG-2999; ARG-3002; LEU-3008; GLU-3016; ARG-3019; ARG-3027; TYR-3028;
LEU-3031; CYS-3035; SER-3036; SER-3037; LEU-3043; LYS-3044; ASP-3049;
HIS-3054; THR-3064 AND GLU-3077.
PubMed=23184949; DOI=10.1074/jbc.M112.396309;
Ahrens S., Geissler B., Satchell K.J.;
"Identification of a His-Asp-Cys catalytic triad essential for
function of the Rho inactivation domain (RID) of Vibrio cholerae MARTX
toxin.";
J. Biol. Chem. 288:1397-1408(2013).
[23]
REVIEW.
PubMed=26185092; DOI=10.1128/microbiolspec.VE-0002-2014;
Satchell K.J.;
"Multifunctional-autoprocessing repeats-in-toxin (MARTX) Toxins of
Vibrios.";
Microbiol. Spectr. 3:0-0(2015).
[24]
FUNCTION (ABH EFFECTOR REGION TOXIN F5).
PubMed=25427654; DOI=10.1111/mmi.12879;
Dolores J.S., Agarwal S., Egerer M., Satchell K.J.;
"Vibrio cholerae MARTX toxin heterologous translocation of beta-
lactamase and roles of individual effector domains on cytoskeleton
dynamics.";
Mol. Microbiol. 95:590-604(2015).
[25]
FUNCTION (ACTIN CROSS-LINKING TOXIN F1 AND ACTIN CROSS-LINKING TOXIN
F4).
PubMed=26228148; DOI=10.1126/science.aab4090;
Heisler D.B., Kudryashova E., Grinevich D.O., Suarez C.,
Winkelman J.D., Birukov K.G., Kotha S.R., Parinandi N.L.,
Vavylonis D., Kovar D.R., Kudryashov D.S.;
"ACD toxin-produced actin oligomers poison formin-controlled actin
polymerization.";
Science 349:535-539(2015).
[26] {ECO:0000244|PDB:3EEB}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 3442-3650 IN COMPLEX WITH
INOSITOL HEXAKISPHOSPHATE, FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING
REPEATS-IN-TOXIN), ENZYME REGULATION, AND MUTAGENESIS OF ASP-3619;
GLU-3620; ARG-3623; LYS-3624; ASP-3632; TRP-3633 AND LYS-3636.
PubMed=18845756; DOI=10.1126/science.1162403;
Lupardus P.J., Shen A., Bogyo M., Garcia K.C.;
"Small molecule-induced allosteric activation of the Vibrio cholerae
RTX cysteine protease domain.";
Science 322:265-268(2008).
[27] {ECO:0000244|PDB:3FZY}
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3440-3650 IN COMPLEX WITH
INOSITOL HEXAKISPHOSPHATE, PARTIAL PROTEIN SEQUENCE, SUBCELLULAR
LOCATION, FUNCTION (MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN
AND CYSTEINE PROTEASE DOMAIN-CONTAINING TOXIN F3), ENZYME REGULATION,
AND CLEAVAGE SITES.
PubMed=19620709; DOI=10.1074/jbc.M109.025510;
Prochazkova K., Shuvalova L.A., Minasov G., Voburka Z., Anderson W.F.,
Satchell K.J.;
"Structural and molecular mechanism for autoprocessing of MARTX toxin
of Vibrio cholerae at multiple sites.";
J. Biol. Chem. 284:26557-26568(2009).
[28] {ECO:0000244|PDB:3GCD}
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 3442-3650 IN COMPLEX WITH
INOSITOL HEXAKISPHOSPHATE AND INHIBITOR, FUNCTION
(MULTIFUNCTIONAL-AUTOPROCESSING REPEATS-IN-TOXIN), ENZYME REGULATION,
CLEAVAGE SITES, AND MUTAGENESIS OF LEU-2447; LEU-3098; LEU-3441 AND
CYS-3581.
PubMed=19465933; DOI=10.1038/nchembio.178;
Shen A., Lupardus P.J., Albrow V.E., Guzzetta A., Powers J.C.,
Garcia K.C., Bogyo M.;
"Mechanistic and structural insights into the proteolytic activation
of Vibrio cholerae MARTX toxin.";
Nat. Chem. Biol. 5:469-478(2009).
-!- FUNCTION: Multifunctional-autoprocessing repeats-in-toxin:
Precursor of a multifunctional toxin that causes destruction of
the actin cytoskeleton by covalent cross-linking of actin and
inactivation of Rho GTPases when translocated into the host
cytoplasm (PubMed:26185092). Upon translocation into the host
cell, undergoes autoprocessing in cis mediated by the peptidase
C80 domain (also named CPD domain): the protease activity is
activated upon binding inositol hexakisphosphate (InsP6) present
at the host cell membrane and delivers the Cysteine protease
domain-containing toxin F3 chain to the host cytosol
(PubMed:17464284, PubMed:18591243, PubMed:18845756,
PubMed:19620709, PubMed:19465933). The Cysteine protease domain-
containing toxin F3 chain will then further cleave and release
effector toxin chains that cause disassembly of the actin
cytoskeleton and enhance V.cholerae colonization of the small
intestine, possibly by facilitating evasion of phagocytic cells
(PubMed:11553575, PubMed:12045243, PubMed:17698573,
PubMed:17698571, PubMed:19812690, PubMed:19620709).
{ECO:0000269|PubMed:11553575, ECO:0000269|PubMed:12045243,
ECO:0000269|PubMed:17464284, ECO:0000269|PubMed:18591243,
ECO:0000269|PubMed:18845756, ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709, ECO:0000269|PubMed:19812690,
ECO:0000303|PubMed:26185092}.
-!- FUNCTION: Cysteine protease domain-containing toxin F3: Following
autocatalytic cleavage in cis at the Leu-3441-Ala-3442 site, this
chain mediates processing in trans to release other individual
toxin chains to the host cytosol (PubMed:19620709). Released
effector toxin chains cause disassembly of the actin cytoskeleton
and enhance V.cholerae colonization of the small intestine,
possibly by facilitating evasion of phagocytic cells
(PubMed:17698573, PubMed:17698571). {ECO:0000269|PubMed:17698571,
ECO:0000269|PubMed:17698573, ECO:0000269|PubMed:19620709}.
-!- FUNCTION: Actin cross-linking toxin F1: Actin-directed toxin that
catalyzes the covalent cross-linking of host cytoplasmic monomeric
actin (PubMed:11032799, PubMed:15199181, PubMed:16954226,
PubMed:17951576, PubMed:19015515, PubMed:19656298,
PubMed:23029200, PubMed:26228148). Mediates the cross-link between
'Lys-50' of one monomer and 'Glu-270' of another actin monomer,
resulting in formation of highly toxic actin oligomers that cause
cell rounding (PubMed:19015515). The toxin can be highly efficient
at very low concentrations by acting on formin homology family
proteins: toxic actin oligomers bind with high affinity to formins
and adversely affect both nucleation and elongation abilities of
formins, causing their potent inhibition in both profilin-
dependent and independent manners (PubMed:26228148). Acts as an
acid--amino-acid ligase that transfers the gamma-phosphoryl group
of ATP to the 'Glu-270' actin residue, resulting in the formation
of an activated acyl phosphate intermediate. This intermediate is
further hydrolyzed and the energy of hydrolysis is utilized for
the formation of the amide bond between actin subunits
(PubMed:23029200). {ECO:0000269|PubMed:11032799,
ECO:0000269|PubMed:15199181, ECO:0000269|PubMed:16954226,
ECO:0000269|PubMed:17951576, ECO:0000269|PubMed:19015515,
ECO:0000269|PubMed:19656298, ECO:0000269|PubMed:23029200,
ECO:0000269|PubMed:26228148}.
-!- FUNCTION: Actin cross-linking toxin F4: Actin-directed toxin that
catalyzes the covalent cross-linking of host cytoplasmic monomeric
actin (PubMed:11032799, PubMed:15199181, PubMed:16954226,
PubMed:17951576, PubMed:19015515, PubMed:19656298,
PubMed:23029200, PubMed:26228148). Mediates the cross-link between
'Lys-50' of one monomer and 'Glu-270' of another actin monomer,
resulting in formation of highly toxic actin oligomers that cause
cell rounding (PubMed:19015515). The toxin can be highly efficient
at very low concentrations by acting on formin homology family
proteins: toxic actin oligomers bind with high affinity to formins
and adversely affect both nucleation and elongation abilities of
formins, causing their potent inhibition in both profilin-
dependent and independent manners (PubMed:26228148). Acts as an
acid--amino-acid ligase that transfers the gamma-phosphoryl group
of ATP to the 'Glu-270' actin residue, resulting in the formation
of an activated acyl phosphate intermediate. This intermediate is
further hydrolyzed and the energy of hydrolysis is utilized for
the formation of the amide bond between actin subunits
(PubMed:23029200). {ECO:0000269|PubMed:11032799,
ECO:0000269|PubMed:15199181, ECO:0000269|PubMed:16954226,
ECO:0000269|PubMed:17951576, ECO:0000269|PubMed:19015515,
ECO:0000269|PubMed:19656298, ECO:0000269|PubMed:23029200,
ECO:0000269|PubMed:26228148}.
-!- FUNCTION: Rho inactivation domain-containing toxin F2: After
delivery to the host cytosol, localizes to the host cell membrane
where it modifies some cellular signaling resulting in loss of all
active GTP-bound Rho and subsequent actin depolymerization.
Although both this chain and the Actin cross-linking toxin F4
chain independently affect polymerized actin, the domains are not
synergistic (PubMed:17474905, PubMed:19434753, PubMed:23184949).
Its similarity with members of the circular permuted thiol
peptidase family, suggests that it acts by mediating modification
of some protein at the host cell membrane (PubMed:26185092).
{ECO:0000269|PubMed:17474905, ECO:0000269|PubMed:19434753,
ECO:0000269|PubMed:23184949, ECO:0000303|PubMed:26185092}.
-!- FUNCTION: ABH effector region toxin F5: Indirectly activates the
small GTPase CDC42. {ECO:0000269|PubMed:25427654}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16954226,
ECO:0000269|PubMed:23029200};
Note=Binds 2 Mg(2+) ions per subunit. Mg(2+) is required for actin
cross-linking activity. Can also use Mn(2+) ions instead of
Mg(2+). {ECO:0000250|UniProtKB:A0A0H3AIG7};
-!- ENZYME REGULATION: Protease activity is inhibited by N-
ethylmaleimide but not other protease inhibitors
(PubMed:17464284). Protease activity is inhibited by aza-leucine
epoxide (PubMed:19465933). Protease activity is activated upon
binding inositol hexakisphosphate (InsP6) via an allosteric
mechanism: the active site is disordered or occluded in the
absence of InsP6, protecting the protease active-site sulfhydryl
until the toxin enters a eukaryotic cell (PubMed:18845756,
PubMed:19620709). Upon processing at the Leu-3441-Ala-3442 site,
the peptidase C80 domain is converted to a form with much reduced
affinity for InsP6, but is reactivated for high affinity binding
of InsP6 by cooperative binding of both a new substrate and InsP6.
Reactivation allows cleavage at other sites, specifically at Leu
residues between the effector domains (PubMed:19620709).
{ECO:0000269|PubMed:17464284, ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933, ECO:0000269|PubMed:19620709}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.8 uM for ATP (for actin cross-linking activity)
{ECO:0000269|PubMed:23029200};
KM=49.9 uM for GTP (for actin cross-linking activity)
{ECO:0000269|PubMed:23029200};
pH dependence:
Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:23029200};
-!- SUBCELLULAR LOCATION: Multifunctional-autoprocessing repeats-in-
toxin: Secreted {ECO:0000269|PubMed:11032799,
ECO:0000269|PubMed:15547287}. Host cytoplasm, host cytosol
{ECO:0000303|PubMed:26185092}. Note=Secreted via the type I
secretion system. {ECO:0000269|PubMed:11032799}.
-!- SUBCELLULAR LOCATION: Rho inactivation domain-containing toxin F2:
Host cell membrane {ECO:0000269|PubMed:20212166,
ECO:0000269|PubMed:22044757}. Note=Targeted to the host cell
membrane via the membrane localization region (MLD).
{ECO:0000269|PubMed:20212166}.
-!- SUBCELLULAR LOCATION: Actin cross-linking toxin F1: Host
cytoplasm, host cytosol {ECO:0000305|PubMed:19620709}.
-!- SUBCELLULAR LOCATION: Actin cross-linking toxin F4: Host
cytoplasm, host cytosol {ECO:0000305|PubMed:19620709}.
-!- SEQUENCE CAUTION:
Sequence=AAD21057.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF119150; AAD21057.1; ALT_INIT; Genomic_DNA.
EMBL; AE003852; AAF94608.1; -; Genomic_DNA.
PIR; C82199; C82199.
RefSeq; NP_231094.1; NC_002505.1.
RefSeq; WP_010895441.1; NC_002505.1.
PDB; 3EEB; X-ray; 2.10 A; A/B=3442-3650.
PDB; 3FZY; X-ray; 1.95 A; A/B=3440-3650.
PDB; 3GCD; X-ray; 2.35 A; A/B/C/D=3442-3650.
PDBsum; 3EEB; -.
PDBsum; 3FZY; -.
PDBsum; 3GCD; -.
ProteinModelPortal; Q9KS12; -.
SMR; Q9KS12; -.
DIP; DIP-48626N; -.
STRING; 243277.VC1451; -.
ESTHER; vibch-rtxAABH; 5_AlphaBeta_hydrolase.
MEROPS; C80.001; -.
EnsemblBacteria; AAF94608; AAF94608; VC_1451.
GeneID; 2613957; -.
KEGG; vch:VC1451; -.
PATRIC; fig|243277.26.peg.1381; -.
eggNOG; ENOG4105EUK; Bacteria.
eggNOG; COG2931; LUCA.
KO; K10953; -.
BioCyc; VCHO:VC1451-MONOMER; -.
SABIO-RK; Q9KS12; -.
EvolutionaryTrace; Q9KS12; -.
Proteomes; UP000000584; Chromosome 1.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0016881; F:acid-amino acid ligase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:TIGR.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:UniProtKB.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
GO; GO:0090527; P:actin filament reorganization; IEA:InterPro.
GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; ISS:TIGR.
GO; GO:0018262; P:isopeptide cross-linking; IDA:UniProtKB.
GO; GO:0018153; P:isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine; IDA:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; ISS:TIGR.
GO; GO:0009405; P:pathogenesis; IDA:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR032074; ACD_dom.
InterPro; IPR020974; CPD_dom.
InterPro; IPR020972; Dermonecrotic/RTX_toxin_MLD.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR022742; Hydrolase_4.
InterPro; IPR011509; RtxA_toxin.
InterPro; IPR011049; Serralysin-like_metalloprot_C.
Pfam; PF16671; ACD; 1.
Pfam; PF12146; Hydrolase_4; 1.
Pfam; PF11647; MLD; 1.
Pfam; PF11713; Peptidase_C80; 1.
Pfam; PF07634; RtxA; 39.
SUPFAM; SSF51120; SSF51120; 2.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS51772; ACD; 1.
PROSITE; PS51771; CGT_MARTX_CPD; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Autocatalytic cleavage; Complete proteome;
Direct protein sequencing; Host cell membrane; Host cytoplasm;
Host membrane; Hydrolase; Ligase; Lipid-binding; Magnesium; Membrane;
Metal-binding; Multifunctional enzyme; Nucleotide-binding; Protease;
Reference proteome; Repeat; Secreted; Signal; Thiol protease; Toxin;
Virulence.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 4558 Multifunctional-autoprocessing repeats-
in-toxin.
/FTId=PRO_0000434113.
CHAIN 33 2447 Actin cross-linking toxin F1.
{ECO:0000305|PubMed:19620709}.
/FTId=PRO_0000434114.
CHAIN 1972 2447 Actin cross-linking toxin F4.
{ECO:0000305|PubMed:19620709}.
/FTId=PRO_0000434115.
CHAIN 2448 3098 Rho inactivation domain-containing toxin
F2. {ECO:0000305|PubMed:19620709}.
/FTId=PRO_0000434116.
CHAIN 3099 3441 ABH effector region toxin F5.
{ECO:0000305|PubMed:19620709}.
/FTId=PRO_0000434117.
CHAIN 3442 4558 Cysteine protease domain-containing toxin
F3. {ECO:0000305|PubMed:19620709}.
/FTId=PRO_0000434118.
REPEAT 114 131 RtxA 1. {ECO:0000255}.
REPEAT 134 151 RtxA 2. {ECO:0000255}.
REPEAT 154 170 RtxA 3. {ECO:0000255}.
REPEAT 174 197 RtxA 4. {ECO:0000255}.
REPEAT 200 217 RtxA 5. {ECO:0000255}.
REPEAT 220 237 RtxA 6. {ECO:0000255}.
REPEAT 268 285 RtxA 7. {ECO:0000255}.
REPEAT 288 304 RtxA 8. {ECO:0000255}.
REPEAT 594 611 RtxA 9. {ECO:0000255}.
REPEAT 614 630 RtxA 10. {ECO:0000255}.
REPEAT 634 651 RtxA 11. {ECO:0000255}.
REPEAT 654 668 RtxA 12. {ECO:0000255}.
REPEAT 751 763 RtxA 13. {ECO:0000255}.
REPEAT 769 781 RtxA 14. {ECO:0000255}.
REPEAT 792 808 RtxA 15. {ECO:0000255}.
REPEAT 811 826 RtxA 16. {ECO:0000255}.
REPEAT 830 845 RtxA 17. {ECO:0000255}.
REPEAT 851 865 RtxA 18. {ECO:0000255}.
REPEAT 868 885 RtxA 19. {ECO:0000255}.
REPEAT 887 901 RtxA 20. {ECO:0000255}.
REPEAT 906 920 RtxA 21. {ECO:0000255}.
REPEAT 925 942 RtxA 22. {ECO:0000255}.
REPEAT 944 960 RtxA 23. {ECO:0000255}.
REPEAT 982 994 RtxA 24. {ECO:0000255}.
REPEAT 1001 1016 RtxA 25. {ECO:0000255}.
REPEAT 1041 1053 RtxA 26. {ECO:0000255}.
REPEAT 1077 1089 RtxA 27. {ECO:0000255}.
REPEAT 1097 1112 RtxA 28. {ECO:0000255}.
REPEAT 1120 1132 RtxA 29. {ECO:0000255}.
REPEAT 1135 1152 RtxA 30. {ECO:0000255}.
REPEAT 1155 1169 RtxA 31. {ECO:0000255}.
REPEAT 1173 1189 RtxA 32. {ECO:0000255}.
REPEAT 1194 1209 RtxA 33. {ECO:0000255}.
REPEAT 1211 1227 RtxA 34. {ECO:0000255}.
REPEAT 1230 1246 RtxA 35. {ECO:0000255}.
REPEAT 1252 1266 RtxA 36. {ECO:0000255}.
REPEAT 1268 1285 RtxA 37. {ECO:0000255}.
REPEAT 1306 1323 RtxA 38. {ECO:0000255}.
REPEAT 1325 1342 RtxA 39. {ECO:0000255}.
DOMAIN 1988 2422 ACD. {ECO:0000255|PROSITE-
ProRule:PRU01108,
ECO:0000305|PubMed:15199181}.
DOMAIN 3462 3646 Peptidase C80. {ECO:0000255|PROSITE-
ProRule:PRU01107}.
NP_BIND 1999 2003 ATP. {ECO:0000250|UniProtKB:A0A0H3AIG7}.
REGION 2574 2658 Membrane localization region (MLD).
{ECO:0000269|PubMed:20212166}.
REGION 2734 3098 Rho inactivation domain (RID).
{ECO:0000305}.
REGION 3195 3310 ABH effector region. {ECO:0000305}.
REGION 3468 3470 Inositol hexakisphosphate binding.
{ECO:0000244|PDB:3EEB,
ECO:0000244|PDB:3FZY,
ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
REGION 3495 3496 Inositol hexakisphosphate binding.
{ECO:0000244|PDB:3EEB,
ECO:0000244|PDB:3FZY,
ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
REGION 3532 3533 Inhibitor binding. {ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:19465933}.
REGION 3610 3612 Inositol hexakisphosphate binding.
{ECO:0000244|PDB:3EEB,
ECO:0000244|PDB:3FZY,
ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
REGION 3616 3618 Inhibitor binding. {ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:19465933}.
REGION 3623 3624 Inositol hexakisphosphate binding.
{ECO:0000244|PDB:3EEB,
ECO:0000244|PDB:3FZY,
ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
COMPBIAS 43 301 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
COMPBIAS 584 1224 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
COMPBIAS 3709 3712 Poly-Ser. {ECO:0000255}.
COMPBIAS 4187 4408 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
ACT_SITE 3532 3532 For cysteine protease activity.
{ECO:0000255|PROSITE-ProRule:PRU01107,
ECO:0000269|PubMed:17698571}.
ACT_SITE 3581 3581 Nucleophile; for cysteine protease
activity. {ECO:0000255|PROSITE-
ProRule:PRU01107,
ECO:0000269|PubMed:17698571}.
METAL 2003 2003 Magnesium 1; catalytic; for actin cross-
linking activity.
{ECO:0000250|UniProtKB:A0A0H3AIG7}.
METAL 2003 2003 Magnesium 2; catalytic; for actin cross-
linking activity.
{ECO:0000250|UniProtKB:A0A0H3AIG7}.
METAL 2065 2065 Magnesium 2; catalytic; for actin cross-
linking activity.
{ECO:0000250|UniProtKB:A0A0H3AIG7}.
METAL 2149 2149 Magnesium 1; catalytic; for actin cross-
linking activity.
{ECO:0000250|UniProtKB:A0A0H3AIG7}.
METAL 2326 2326 Magnesium 1; catalytic; for actin cross-
linking activity.
{ECO:0000250|UniProtKB:A0A0H3AIG7}.
BINDING 2255 2255 ATP; via carbonyl oxygen.
{ECO:0000250|UniProtKB:A0A0H3AIG7}.
BINDING 3526 3526 Inositol hexakisphosphate.
{ECO:0000244|PDB:3EEB,
ECO:0000244|PDB:3FZY,
ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
BINDING 3577 3577 Inositol hexakisphosphate.
{ECO:0000244|PDB:3EEB,
ECO:0000244|PDB:3FZY,
ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
BINDING 3581 3581 Inhibitor. {ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:19465933}.
BINDING 3636 3636 Inositol hexakisphosphate.
{ECO:0000244|PDB:3EEB,
ECO:0000244|PDB:3FZY,
ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
BINDING 3641 3641 Inositol hexakisphosphate.
{ECO:0000244|PDB:3EEB,
ECO:0000244|PDB:3FZY,
ECO:0000244|PDB:3GCD,
ECO:0000269|PubMed:18845756,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
SITE 1971 1972 Cleavage; by autolysis.
{ECO:0000269|PubMed:19620709}.
SITE 2447 2448 Cleavage; by autolysis.
{ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
SITE 3098 3099 Cleavage; by autolysis.
{ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
SITE 3441 3442 Cleavage; by autolysis.
{ECO:0000269|PubMed:17464284,
ECO:0000269|PubMed:18591243,
ECO:0000269|PubMed:19465933,
ECO:0000269|PubMed:19620709}.
MUTAGEN 2003 2003 E->A: Abolished actin cross-linking
activity and ability to round host cells.
{ECO:0000269|PubMed:19656298}.
MUTAGEN 2005 2005 E->A: Impaired actin cross-linking
activity and ability to round host cells.
{ECO:0000269|PubMed:19656298}.
MUTAGEN 2005 2005 E->G: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2035 2035 L->P: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2038 2038 D->A: Impaired actin cross-linking
activity and ability to round host cells.
{ECO:0000269|PubMed:19656298}.
MUTAGEN 2055 2055 G->E: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2065 2065 E->A: Abolished actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2065 2065 E->G: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2068 2068 T->P: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2089 2089 L->P: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2096 2096 H->A: Abolished actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2117 2117 L->P: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2149 2149 Q->R: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2153 2153 A->T: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2175 2175 W->R: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2206 2206 L->P: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2209 2209 V->A: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2250 2250 W->R: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2259 2259 V->I: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2326 2326 E->A: Abolished actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2328 2328 R->A: Impaired actin cross-linking
activity and ability to round host cells.
{ECO:0000269|PubMed:19656298}.
MUTAGEN 2328 2328 R->H: Reduced actin cross-linking
activity. {ECO:0000269|PubMed:19656298}.
MUTAGEN 2447 2447 L->A: Impaired cleavage of the Rho
inactivation domain-containing toxin F2
chain; when associated with A-3098.
{ECO:0000269|PubMed:19465933}.
MUTAGEN 2596 2596 Y->F: Abolished localization to the host
cell membrane.
{ECO:0000269|PubMed:20212166}.
MUTAGEN 2641 2641 S->T: Abolished localization to the host
cell membrane.
{ECO:0000269|PubMed:20212166}.
MUTAGEN 2643 2643 R->K: Abolished localization to the host
cell membrane.
{ECO:0000269|PubMed:20212166}.
MUTAGEN 2734 2734 E->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2735 2735 Y->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2760 2760 D->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2764 2764 L->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2766 2766 K->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2768 2768 H->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2772 2772 E->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2776 2776 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2779 2779 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2781 2781 T->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2786 2786 K->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2788 2788 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2790 2790 H->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2791 2791 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2793 2793 L->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2795 2795 H->A: Impaired activity of the Rho
inactivation domain-containing toxin F2
chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2798 2798 L->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2804 2804 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2820 2820 Y->A: Impaired activity of the Rho
inactivation domain-containing toxin F2
chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2820 2820 Y->F: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2822 2822 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2829 2829 K->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2830 2830 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2850 2850 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2864 2864 L->A: Impaired activity of the Rho
inactivation domain-containing toxin F2
chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2867 2867 D->A: Impaired activity of the Rho
inactivation domain-containing toxin F2
chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2871 2871 E->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2872 2872 E->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2874 2874 D->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2887 2887 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2914 2914 L->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2950 2950 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2956 2956 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2961 2961 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2971 2971 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2977 2977 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2981 2981 E->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2982 2982 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2991 2991 K->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2993 2993 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2996 2996 D->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 2999 2999 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3002 3002 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3005 3005 L->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3008 3008 L->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3016 3016 E->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3019 3019 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3027 3027 R->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3028 3028 Y->A: Impaired activity of the Rho
inactivation domain-containing toxin F2
chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3028 3028 Y->F: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3031 3031 L->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3035 3035 C->A,S: Impaired activity of the Rho
inactivation domain-containing toxin F2
chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3036 3036 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3037 3037 S->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3043 3043 L->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3044 3044 K->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3049 3049 D->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3054 3054 H->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3064 3064 T->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3077 3077 E->A: Does not affect the activity of the
Rho inactivation domain-containing toxin
F2 chain. {ECO:0000269|PubMed:23184949}.
MUTAGEN 3098 3098 L->A: Impaired cleavage of the Rho
inactivation domain-containing toxin F2
chain; when associated with A-2447.
{ECO:0000269|PubMed:19465933}.
MUTAGEN 3441 3441 L->A: Modified autocatalytic cleavage
site, leading to cleavage at another
site. {ECO:0000269|PubMed:19465933}.
MUTAGEN 3462 3462 P->A: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3470 3470 R->A: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3476 3476 I->A: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3478 3478 Q->A: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3480 3480 E->A: No effect in autocatalytic
cleavage. Impaired autocatalytic
cleavage; when associated with A-3482.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3482 3482 D->A: No effect in autocatalytic
cleavage. Impaired autocatalytic
cleavage; when associated with A-3480.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3488 3488 A->I: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3492 3492 L->D: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3495 3495 K->A: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3499 3500 SS->AA: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3524 3524 K->A: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3526 3526 R->A: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3532 3532 H->A: Abolishes autocatalytic cleavage.
{ECO:0000269|PubMed:17464284,
ECO:0000269|PubMed:18591243}.
MUTAGEN 3534 3534 R->A: Increased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3537 3537 S->A: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3551 3551 E->A: Does not affect autocatalytic
cleavage. {ECO:0000269|PubMed:17464284}.
MUTAGEN 3552 3552 L->A: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3572 3572 K->A: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3581 3581 C->S,A: Abolishes autocatalytic cleavage.
{ECO:0000269|PubMed:17464284,
ECO:0000269|PubMed:18591243,
ECO:0000269|PubMed:19465933}.
MUTAGEN 3606 3606 R->A: Increased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3609 3609 V->A: No effect in autocatalytic
cleavage. {ECO:0000269|PubMed:18591243}.
MUTAGEN 3612 3612 R->A: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3619 3619 D->A,N: Slightly reduced inositol
hexakisphosphate-binding and strongly
decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18845756}.
MUTAGEN 3620 3620 E->A: Does not affect inositol
hexakisphosphate-binding.
{ECO:0000269|PubMed:18845756}.
MUTAGEN 3623 3623 R->A: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3623 3623 R->Q: Slightly reduced inositol
hexakisphosphate-binding and strongly
decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18845756}.
MUTAGEN 3624 3624 K->A: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
MUTAGEN 3624 3624 K->N: Abolishes inositol
hexakisphosphate-binding and
autocatalytic cleavage.
{ECO:0000269|PubMed:18845756}.
MUTAGEN 3632 3632 D->A: Does not affect inositol
hexakisphosphate-binding.
{ECO:0000269|PubMed:18845756}.
MUTAGEN 3633 3633 W->A: Reduced inositol hexakisphosphate-
binding and autocatalytic cleavage.
{ECO:0000269|PubMed:18845756}.
MUTAGEN 3633 3633 W->F: Slightly reduced inositol
hexakisphosphate-binding and strongly
decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18845756}.
MUTAGEN 3636 3636 K->N: Abolishes inositol
hexakisphosphate-binding and
autocatalytic cleavage.
{ECO:0000269|PubMed:18845756}.
MUTAGEN 3641 3641 K->A: Decreased autocatalytic cleavage.
{ECO:0000269|PubMed:18591243}.
HELIX 3452 3454 {ECO:0000244|PDB:3FZY}.
STRAND 3472 3478 {ECO:0000244|PDB:3FZY}.
HELIX 3483 3495 {ECO:0000244|PDB:3FZY}.
HELIX 3496 3499 {ECO:0000244|PDB:3FZY}.
STRAND 3500 3505 {ECO:0000244|PDB:3FZY}.
STRAND 3511 3516 {ECO:0000244|PDB:3FZY}.
HELIX 3518 3520 {ECO:0000244|PDB:3FZY}.
STRAND 3523 3530 {ECO:0000244|PDB:3FZY}.
STRAND 3533 3535 {ECO:0000244|PDB:3FZY}.
HELIX 3549 3567 {ECO:0000244|PDB:3FZY}.
STRAND 3574 3582 {ECO:0000244|PDB:3FZY}.
STRAND 3588 3591 {ECO:0000244|PDB:3FZY}.
HELIX 3592 3602 {ECO:0000244|PDB:3FZY}.
STRAND 3608 3614 {ECO:0000244|PDB:3FZY}.
STRAND 3616 3618 {ECO:0000244|PDB:3FZY}.
STRAND 3624 3627 {ECO:0000244|PDB:3FZY}.
STRAND 3629 3631 {ECO:0000244|PDB:3FZY}.
STRAND 3633 3636 {ECO:0000244|PDB:3FZY}.
HELIX 3638 3640 {ECO:0000244|PDB:3FZY}.
STRAND 3641 3644 {ECO:0000244|PDB:3FZY}.
SEQUENCE 4558 AA; 485355 MW; 800DD5D1D119AE19 CRC64;
MVFYLIPKRR VWLMGKPFWR SVEYFFTGNY SADDGNNNIV AIGFGGQIHA YGGDDHVTVG
SIGATVYTGS GNDTVVGGSA YLKVEDSTGH LIVKGAAGYA DINKSGDGNV SFAGAAGGVS
IDHLGNHGDV SYGGAAAYNG ITRKGLSGNV TFAGAGGYNA LWHETNQGNL SFTGAGAGNK
LDRTWSNRYQ GSHGDVTFDG AGAANSISSR VETGNITFRG AGADNHLVRK GKVGDITLQG
AGASNRIERT HQAEDVYTQT RGNIRFEGVG GYNSLYSDVA HGDIHFSGGG AYNTIIRKGS
GNDFAKEGMT NAKADEIVLT KAVMSGSWIG QDHHVTAVKS ASEPNTYLFA FADSTYTKIN
KVQLRNDPQT GELKYYSTAW YKEVNHLSNL ANQDISDNGG FTAVNINGAY TLSDLKVEHQ
QSVTVHAVEK SLTEYEWVTY ANGAVIDAKE VSLSDAKMGG HAIYADGTKV DVKAVKSNRQ
PNTYIYAKVL GPYTKIVVVE LANDPETGAL KYQARSWYKE GDHTANIANQ DISSATGYNP
MGKGGYSLSD LHYSVNAVRS TSETVADIEE YTDQTLFKPA NDSGESSGDV RFNGAGGGNV
IKSNVTRGNV HFNGGGIANV ILHSSQFGNT EFNGGGAANV IVKSGEEGDL TFRGAGLANV
LVHQSEQGKM DVYAGGAVNV LVRLGDGQYL AHLLAYGNIS VQKGSGDSRV VMLGGYNTHT
QIGSGNGLWL AAGGFNVMTQ VGKGDVAAVL AGGANVLTKM GEGELTSGML GGANVITHIS
NDDQLSNTTA VALGGANILT KKGKGNTLAV MGGGANVLTH VGDGTTTGVM VGGANILTKV
GNGDTTGILL GVGNVLTHVG DGQTLGVMGA AGNIFTKVGD GTSIAVMIGA GNIFTHVGEG
NAWALMGGLG NVFTKVGNGD ALALMVAEAN VFTHIGDGMS VALMLAKGNV ATKVGNGTTL
AAMVGNVNIF THIGHGSTFA AMIGQANIMT KVGNDLTAAL MVGKANIMTH VGDGTSLGLF
AGEVNVMTKV GNGTTLAAMF GKANIMTHVG DGLTGVLALG EANIVTKLGD DFMGVVAAAK
ANVVTHVGDA TTAAVLAGKG NILTKVGEGT TVGLLISDVG NVMTHVGDGT TIGIAKGKAN
LITKVGDGLG VNVTWGQANV FTQVGDGDRY NFAKGEANLI TKVGDGQEVS VVQGEANIIT
HVGNGDDYTG AWGKANVITK VGHGQNVVLA KGEANIVTQV GDGDSFNALW SKGNIVTKVG
DGMQVTAAKG QANITTTVGN GLNVTAAYGD ANINTKVGDG VSVNVAWGKY NINTKVGDGL
NVAVMKGKAN ANIHVGDGLN INASYAQNNV AIKVGNGDFY SLAVASSNTS SNKLSALFDN
IKQTVLGVGG SQAINYLVQG DEASSSGTHK GRGAIATPEI TKLDGFQMDA IKEVSSDLGD
SLTGSVTKVD TPDLNKMQHA LNVDDSSVQA PNLIVNGDFE LGEHGWQSTH GVEASYAGSV
YGVEGEGHGA RVTELDTYTN TSLYQDLANL AQGEVIAVSF DFAKRAGLSN NEGIEVLWNG
EVVFSSSGDE SAWQQKNLKL TAQAGSNRIE FKGTGHNDGL GYILDNVVAT SESSQQANAI
REHATQNPAA QNALSDKERA EADRQRLEQE KQKQLDAVAG SQSQLESTDQ QALENNGQAQ
RDAVKEESEA VTAELAKLAQ GLDVLDGQAT HTGESGDQWR NDFAGGLLDG VQSQLDDAKQ
LANDKIAAAK QTLSDNNSKV KESVAKSEAG VAQGEQNRAG VEQDIADAQA DAEKRKADAL
AKGKDAQQAE SDAHHAVNNA QSRGDRDVQL AENKANQAQA DAQGAKQNEG DRPDRQGVTG
SGLSGNAHSV EGAGETDSHV NTDSQTNADG RFSEGLTEQE QEALEGATNA VNRLQINAGI
RAKNSVSSMT SMFSETNSKS IVVPTKVSPE PERQEVTRRD VRISGVNLES LSAVQGSQPT
GQLASKSVPG FKSHFASTSI GIENELSGLV VVLPKNSAQT FGYVHDSQGN PLFMLTKDMN
QGGYSNPVGI NDIQGVNNWQ THTIELVTYP SEISDTAAVE SRKEAMLWLA KEFTDHINQS
NHQSLPHLVS DDGRFTLVIS NSKHLIAAGN GTSIDAQGKT IGMTPSGQQA TMAISAKEFG
TSSSPEVRLL ESAPWYQAGL RDEFLANAKN TTLDDPATAQ NVYAYLTSVY SKTADLAKEY
GIYINDWDPA SEGFSPNAQG LTDPKVKNAW SILPRTKPVR MLELLSAEDS RYVRQQIAEK
LKGTYSESLA KNVFEYFQYG GEVAGHGINN ATTGSVQQPE PAILFEFRSV PSALSDFVPK
TASTVKVDVK ALDHFDSASR KAIITEVNAL VSGSEDFDAW YQEYRASKGQ PPVKNPKSSA
SANHKAEWLM TQHAEQWAKI TAPYTDNHET LTSTKLASND KEELHALGET SNLENNKQQE
NVASIINTML NDMLPFYALR TERNLLVQEG DEGFEVRAWP GTEDKSKTII LEDPEDAAQH
KAIERFILAN FDNFEQMPDE LFLVDNKVIS HHEGRTHVLA QKVDGAWQYN ATVELMSVTE
LLDAANVTGK IRGESYQQVI DALTDYHASI TEHADYEPES VEKLLNLRKK IEGYVLGHPD
SGRVEAMNSL LNQVNTRLDE VSLLSVAEQT IQAQNSFSRL YDQLEAANLK ESKHLYLDQN
GDFVTKGKGN LANIDLLGSR EAVLEKVKLT VSNEYGQTVA DTIFAGLSAK DLAKDGKGVD
IAGLNKVHQA IEQHLSPVSA TLYIWKPSDH SALGHAALQI GQGRTQLEGQ AAADFNQQNY
VSWWPLGSKS SNISNILNVA TKDQPDLKLR WSDFSQPAHQ NDTLEHDVAS EENDGFGLHD
GDIKLKRFIE KLNAAKGIDA SFKEASEGYA SVLLGNPDML ETTSIPAHVF QPFVEQWNDT
SYDMMDVAHR FAQELRLQAQ RSDDPELLEK RIGNVIRQFA ERALEEIETF KASQADQGRV
FRINLEGLDV AAMQAEWHRL SNDPDARYQL LTKNCSSTVA KVLKAGGADK LIGHTWLPKF
GVWTPTELFN FGQALQEAQL EIAAKKQSHQ VTDVLDALSG NEKPKENVAI ENDGTPPRDK
ESLSPLTRFL NNELYGDKEA RRKIGEITQT LLDHAVEKGE SQKITLQGEA GRLTGYYHQG
TAPSEGETSS PSGKVVLFLH GSGSSAEEQA SAIRNHYQKQ GIDMLAVNLR GYGESDGGPS
EKGLYQDART MFNYLVNDKG IDPSNIIIHG YSMGGPIAAD LARYAAQNGQ AVSGLLLDRP
MPSMTKAITA HEVANPAGIV GAIAKAVNGQ FSVEKNLEGL PKETSILLLT DNEGLGNEGE
KLRTKLTASG YNVTGEQTFY GHEASNRLMS QYADQIVSGL SSSASVDEDL DQQGLDTTST
KDQGISNKND HLQVVDSKEA LADGKILHNQ NVNSWGPITV TPTTDGGETR FDGQIIVQME
NDPVVAKAAA NLAGKHAESS VVVQLDSDGN YRVVYGDPSK LDGKLRWQLV GHGRDHSETN
NTRLSGYSAD ELAVKLAKFQ QSFNQAENIN NKPDHISIVG CSLVSDDKQK GFGHQFINAM
DANGLRVDVS VRSSELAVDE AGRKHTKDAN GDWVQKAENN KVSLSWDAQG EVVAKDERIR
NGIAEGDIDL SRIGVNNVDE PARGAIGDNN DVFDAPEKRK PETEVIANSS SSNQFSYSGN
IQVNVGEGEF TAVNWGTSNV GIKVGTGGFK SLAFGDNNVM VHIGDGESKH SVDIGGYQAL
EGAQMFLGNR NVSFNFGHSN DLILMMDKSI PTPPLVNPFD GAARISGVLQ GIATSGEGED
WLAAQEQQWT LSGAKKFVKD MSGLDQSSSV DYTTLVELDS QNERDSRGLK HDAEATLNKQ
YNQWLSGNGN SGTSQLSRAD KLRQANEKLA FNFAVGGQGA DIQVTTGNWN FMFGDNIQSI
LDTNLGSLFG LMTQQFTATG QAKTTFTYTP QDLPRQLKNK LLGQLAGVGA ETTLADIFGV
DYTASGQIVS RNGQAVDGVA ILKEMLEVIG EFSGDQLQAF VDPAKLLDSL KAGIDMGADG
IKSFAETHGL KEKAPEEEKD NSSVSVNGAN VNSAQGATVA DGNTETAETQ DRAFGFNSLN
LPNLFATIFS QDKQKEMKSL VENLKQNLTA DLLNMKEKTF DFLRNSGHLQ GDGDINISLG
NYNFNWGGDG KDLGAYLGDN NNFWGGRGDD VFYATGKSNI FTGGEGNDMG VLMGRENMMF
GGDGNDTAVV AGRINHVFLG AGDDQSFVFG EGGEIDTGSG RDYVVTSGNF NRVDTGDDQD
YSVTIGNNNQ VELGAGNDFA NIFGNYNRIN AGAGNDVVKL MGYHAVLNGG DGDDHLIATA
ISKFSQFNGG EGRDLMVLGG YQNTFKGGTD VDSFVVSGDV IDNLVEDIRS EDNIVFNGID
WQKLWFERSG YDLKLSILRD PSNDSDQSKF EHIGSVTFSD YFNGNRAQVV IGMSEKDLSG
EREYTMLSDS AIDALVQAMS GFEPQAGDNG FIDSLESKSQ AAISMAWSDV VHKKGLMV


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