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Protective antigen (PA) (Anthrax toxins translocating protein) (PA-83) (PA83) [Cleaved into: Protective antigen PA-20 (PA20); Protective antigen PA-63 (PA63)]

 PAG_BACAN               Reviewed;         764 AA.
P13423; Q937W2; Q937W3; Q9F5R7; Q9KH69; Q9RQU2;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
30-AUG-2017, entry version 172.
RecName: Full=Protective antigen;
Short=PA;
AltName: Full=Anthrax toxins translocating protein;
AltName: Full=PA-83;
Short=PA83;
Contains:
RecName: Full=Protective antigen PA-20;
Short=PA20;
Contains:
RecName: Full=Protective antigen PA-63;
Short=PA63;
Flags: Precursor;
Name=pagA; Synonyms=pag;
OrderedLocusNames=pXO1-110, BXA0164, GBAA_pXO1_0164;
Bacillus anthracis.
Plasmid pXO1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1392;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3148491; DOI=10.1016/0378-1119(88)90439-8;
Welkos S.L., Lowe J.R., Eden-Mccutchan F., Vodkin M., Leppla S.H.,
Schmidt J.J.;
"Sequence and analysis of the DNA encoding protective antigen of
Bacillus anthracis.";
Gene 69:287-300(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=28, 33, BA1024, and BA1035;
PubMed=10197996;
Price L.B., Hugh-Jones M., Jackson P.J., Keim P.;
"Genetic diversity in the protective antigen gene of Bacillus
anthracis.";
J. Bacteriol. 181:2358-2362(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=V770-NP1-R / ATCC 14185;
PubMed=10899854; DOI=10.1128/IAI.68.8.4549-4558.2000;
Cohen S., Mendelson I., Altboum Z., Kobiler D., Elhanany E., Bino T.,
Leitner M., Inbar I., Rosenberg H., Gozes Y., Barak R., Fisher M.,
Kronman C., Velan B., Shafferman A.;
"Attenuated nontoxinogenic and nonencapsulated recombinant Bacillus
anthracis spore vaccines protect against anthrax.";
Infect. Immun. 68:4549-4558(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Sterne;
PubMed=10515943;
Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K.,
Keim P., Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D.,
Martinez Y., Ricke D., Svensson R., Jackson P.J.;
"Sequence and organization of pXO1, the large Bacillus anthracis
plasmid harboring the anthrax toxin genes.";
J. Bacteriol. 181:6509-6515(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Ames / isolate Florida / A2012;
PubMed=12004073; DOI=10.1126/science.1071837;
Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L.,
Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D.,
Keim P., Fraser C.M.;
"Comparative genome sequencing for discovery of novel polymorphisms in
Bacillus anthracis.";
Science 296:2028-2033(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ames ancestor;
PubMed=18952800; DOI=10.1128/JB.01347-08;
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
J. Bacteriol. 191:445-446(2009).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-751.
STRAIN=Carbosap, and Ferrara;
PubMed=12067380; DOI=10.1046/j.1365-2672.2002.01660.x;
Adone R., Pasquali P., La Rosa G., Marianelli C., Muscillo M.,
Fasanella A., Francia M., Ciuchini F.;
"Sequence analysis of the genes encoding for the major virulence
factors of Bacillus anthracis vaccine strain 'Carbosap'.";
J. Appl. Microbiol. 93:117-121(2002).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-434.
STRAIN=PAI;
PubMed=14985634;
Inoue S., Noguchi A., Tanabayashi K., Yamada A.;
"Preparation of a positive control DNA for molecular diagnosis of
Bacillus anthracis.";
Jpn. J. Infect. Dis. 57:29-32(2004).
[9]
DOMAINS.
PubMed=1651334;
Singh Y., Klimpel K.R., Quinn C.P., Chaudhary V.K., Leppla S.H.;
"The carboxyl-terminal end of protective antigen is required for
receptor binding and anthrax toxin activity.";
J. Biol. Chem. 266:15493-15497(1991).
[10]
CHARACTERIZATION.
STRAIN=Sterne;
PubMed=8051159;
Milne J.C., Furlong D., Hanna P.C., Wall J.S., Collier R.J.;
"Anthrax protective antigen forms oligomers during intoxication of
mammalian cells.";
J. Biol. Chem. 269:20607-20612(1994).
[11]
CHARACTERIZATION.
PubMed=11207581; DOI=10.1046/j.1462-5822.2000.00052.x;
Beauregard K.E., Collier R.J., Swanson J.A.;
"Proteolytic activation of receptor-bound anthrax protective antigen
on macrophages promotes its internalization.";
Cell. Microbiol. 2:251-258(2000).
[12]
TOXIN REGULATION.
STRAIN=Weybridge;
PubMed=8300513; DOI=10.1128/jb.176.3.586-595.1994;
Koehler T.M., Dai Z., Kaufman-Yarbray M.;
"Regulation of the Bacillus anthracis protective antigen gene: CO2 and
a trans-acting element activate transcription from one of two
promoters.";
J. Bacteriol. 176:586-595(1994).
[13]
FOLDING BY PSRA.
PubMed=12606539; DOI=10.1074/jbc.M301244200;
Williams R.C., Rees M.L., Jacobs M.F., Pragai Z., Thwaite J.E.,
Baillie L.W., Emmerson P.T., Harwood C.R.;
"Production of Bacillus anthracis protective antigen is dependent on
the extracellular chaperone, PrsA.";
J. Biol. Chem. 278:18056-18062(2003).
[14]
INTERACTION WITH ANTHRAX TOXIN RECEPTOR.
PubMed=14507921; DOI=10.1074/jbc.M307900200;
Bradley K.A., Mogridge J., Jonah G., Rainey G.J.A., Batty S.,
Young J.A.T.;
"Binding of anthrax toxin to its receptor is similar to alpha
integrin-ligand interactions.";
J. Biol. Chem. 278:49342-49347(2003).
[15]
MUTAGENESIS OF 342-PHE-PHE-343 AND ASP-344.
STRAIN=Sterne;
PubMed=7961869;
Singh Y., Klimpel K.R., Arora N., Sharma M., Leppla S.H.;
"The chymotrypsin-sensitive site, FFD315, in anthrax toxin protective
antigen is required for translocation of lethal factor.";
J. Biol. Chem. 269:29039-29046(1994).
[16]
MUTAGENESIS OF DOMAIN 4 LOOPS.
STRAIN=Sterne;
PubMed=10085028;
Varughese M., Teixeira A.V., Liu S., Leppla S.H.;
"Identification of a receptor-binding region within domain 4 of the
protective antigen component of anthrax toxin.";
Infect. Immun. 67:1860-1865(1999).
[17]
MUTAGENESIS OF TRP-375; MET-379 AND LEU-381.
STRAIN=Sterne;
PubMed=11178978; DOI=10.1006/bbrc.2001.4320;
Batra S., Gupta P., Chauhan V., Singh A., Bhatnagar R.;
"Trp 346 and Leu 352 residues in protective antigen are required for
the expression of anthrax lethal toxin activity.";
Biochem. Biophys. Res. Commun. 281:186-192(2001).
[18]
MUTAGENESIS OF PHE-581; PHE-583; ILE-591; LEU-595 AND ILE-603.
STRAIN=Sterne;
PubMed=11554763; DOI=10.1006/bbrc.2001.5613;
Ahuja N., Kumar P., Bhatnagar R.;
"Hydrophobic residues Phe552, Phe554, Ile562, Leu566, and Ile574 are
required for oligomerization of anthrax protective antigen.";
Biochem. Biophys. Res. Commun. 287:542-549(2001).
[19]
MUTAGENESIS OF PRO-289.
STRAIN=Sterne;
PubMed=11356563; DOI=10.1111/j.1574-6968.2001.tb10646.x;
Khanna H., Chopra A.P., Arora N., Chaudhry A., Singh Y.;
"Role of residues constituting the 2beta1 strand of domain II in the
biological activity of anthrax protective antigen.";
FEMS Microbiol. Lett. 199:27-31(2001).
[20]
MUTAGENESIS OF GLN-512; ASP-541; LEU-543 AND ARG-621.
PubMed=11222612; DOI=10.1128/JB.183.6.2111-2116.2001;
Mogridge J., Mourez M., Collier R.J.;
"Involvement of domain 3 in oligomerization by the protective antigen
moiety of anthrax toxin.";
J. Bacteriol. 183:2111-2116(2001).
[21]
MUTAGENESIS OF LYS-426; ASP-454 AND PHE-456.
PubMed=11113126; DOI=10.1074/jbc.M008309200;
Sellman B.R., Nassi S., Collier R.J.;
"Point mutations in anthrax protective antigen that block
translocation.";
J. Biol. Chem. 276:8371-8376(2001).
[22]
MUTAGENESIS OF PRO-213; LEU-216; PHE-231; LEU-232; PRO-234; ILE-236;
ILE-239; TRP-255 AND PHE-265.
STRAIN=Sterne;
PubMed=12117959; DOI=10.1128/IAI.70.8.4477-4484.2002;
Chauhan V., Bhatnagar R.;
"Identification of amino acid residues of anthrax protective antigen
involved in binding with lethal factor.";
Infect. Immun. 70:4477-4484(2002).
[23]
MUTAGENESIS OF ILE-393; THR-409; SER-411; THR-422; LYS-426; ASN-428;
TYR-440; ASN-451; ASP-454 AND PHE-456.
PubMed=14623961; DOI=10.1073/pnas.2436299100;
Mourez M., Yan M., Lacy D.B., Dillon L., Bentsen L., Marpoe A.,
Maurin C., Hotze E., Wigelsworth D., Pimental R.-A., Ballard J.D.,
Collier R.J., Tweten R.K.;
"Mapping dominant-negative mutations of anthrax protective antigen by
scanning mutagenesis.";
Proc. Natl. Acad. Sci. U.S.A. 100:13803-13808(2003).
[24]
MUTAGENESIS OF ASN-686; LYS-708; LYS-709; TYR-710; ASN-711; ASP-712;
LYS-713; LEU-714; PRO-715; LEU-716; TYR-717; ILE-718; ASN-720; PRO-721
AND ASN-722.
PubMed=12771151; DOI=10.1074/jbc.M301154200;
Rosovitz M.J., Schuck P., Varughese M., Chopra A.P., Mehra V.,
Singh Y., McGinnis L.M., Leppla S.H.;
"Alanine-scanning mutations in domain 4 of anthrax toxin protective
antigen reveal residues important for binding to the cellular receptor
and to a neutralizing monoclonal antibody.";
J. Biol. Chem. 278:30936-30944(2003).
[25]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=9039918; DOI=10.1038/385833a0;
Petosa C., Collier R.J., Klimpel K.R., Leppla S.H., Liddington R.C.;
"Crystal structure of the anthrax toxin protective antigen.";
Nature 385:833-838(1997).
[26]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-764 IN COMPLEX WITH
ANTXR2.
PubMed=15243628; DOI=10.1038/nature02763;
Santelli E., Bankston L.A., Leppla S.H., Liddington R.C.;
"Crystal structure of a complex between anthrax toxin and its host
cell receptor.";
Nature 430:905-908(2004).
[27]
X-RAY CRYSTALLOGRAPHY (4.3 ANGSTROMS) OF 203-764 IN COMPLEX WITH
ANTXR2.
PubMed=15326297; DOI=10.1073/pnas.0405405101;
Lacy D.B., Wigelsworth D.J., Melnyk R.A., Harrison S.C., Collier R.J.;
"Structure of heptameric protective antigen bound to an anthrax toxin
receptor: a role for receptor in pH-dependent pore formation.";
Proc. Natl. Acad. Sci. U.S.A. 101:13147-13151(2004).
[28]
REVIEW.
PubMed=11544370; DOI=10.1146/annurev.micro.55.1.647;
Mock M., Fouet A.;
"Anthrax.";
Annu. Rev. Microbiol. 55:647-671(2001).
-!- FUNCTION: One of the three proteins composing the anthrax toxin,
the agent which infects many mammalian species and that may cause
death. PA binds to a receptor (ATR) in sensitive eukaryotic cells,
thereby facilitating the translocation of the enzymatic toxin
components, edema factor and lethal factor, across the target cell
membrane. PA associated with LF causes death when injected, PA
associated with EF produces edema. PA induces immunity to
infection with anthrax.
-!- SUBUNIT: Anthrax toxins are composed of three distinct proteins, a
protective antigen (PA), a lethal factor (LF) and an edema factor
(EF). None of these is toxic by itself. PA+LF forms the lethal
toxin (LeTx); PA+EF forms the edema toxin (EdTx). PA-63 forms
heptamers and this oligomerization is required for LF or EF
binding. This complex is endocytosed by the host. Once activated,
at low pH, the heptamer undergoes conformational changes and
converts from prepore to pore inserted in the membrane, forming
cation-selective channels and triggering the release of LF and EF
in the host cytoplasm. {ECO:0000269|PubMed:15243628,
ECO:0000269|PubMed:15326297}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-456868, EBI-456868;
Q9H6X2-2:ANTXR1 (xeno); NbExp=3; IntAct=EBI-456868, EBI-905659;
P58335:ANTXR2 (xeno); NbExp=7; IntAct=EBI-456868, EBI-456840;
P15917:lef; NbExp=5; IntAct=EBI-456868, EBI-456923;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space. Note=Secreted
through the Sec-dependent secretion pathway. Therefore, PA is
translocated across the membrane in an unfolded state and then it
is folded into its native configuration on the trans side of the
membrane, prior to its release to the environment. PA requires the
extracellular chaperone PrsA for efficient folding.
-!- DOMAIN: The molecule is folded into four functional domains. Each
domain is required for a particular step in the toxicity process.
Domain 1 contains two calcium ions and the proteolytic activation
site. Cleavage of the PA monomer releases the subdomain 1a, which
is the N-terminal fragment of 20-kDa (PA20). The subdomain 1b is
part of the remaining 63-kDa fragment (PA63) and contains the
binding sites for LP and EF. Domain 2 is a beta-barrel core
containing a large flexible loop that has been implicated in
membrane insertion and pore formation. There is a chymotrypsin
cleavage site in this loop that is required for toxicity. Domain 3
has a hydrophobic patch thought to be involved in protein-protein
interactions. Domain 4 appears to be a separate domain and shows
limited contact with the other three domains: it would swing out
of the way during membrane insertion. It is required for binding
to the receptor; the small loop is involved in receptor
recognition. {ECO:0000269|PubMed:1651334}.
-!- PTM: Proteolytic activation by furin or a furin-like protease
cleaves the protein in two parts, PA-20 and PA-63; the latter is
the mature protein. The cleavage occurs at the cell surface and
probably in the serum of infected animals as well; both native and
cleaved PA are able to bind to the cell receptor. The release of
PA20 from the remaining receptor-bound PA63 exposes the binding
site for EF and LF, and promotes oligomerization and
internalization of the protein.
-!- MISCELLANEOUS: In PubMed:10085028 multiple mutagenesis experiments
were performed that showed that the residues present in the small
loop of domain 4, and not the ones in the large loop, are involved
in receptor recognition. In PubMed:14623961 high-throughput
scanning mutagenesis experiments were performed in which all
residues of PA-63 were mutated into Cys. Dominantly negative (DN)
mutants were all clustered in domain 2. DN mutants prevent the
conformational transition of PA-63 from the prepore to the pore
state.
-!- SIMILARITY: Belongs to the bacterial binary toxin family.
{ECO:0000305}.
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EMBL; M22589; AAA22637.1; -; Genomic_DNA.
EMBL; AF306778; AAG24446.1; -; Genomic_DNA.
EMBL; AF306779; AAG24447.1; -; Genomic_DNA.
EMBL; AF306780; AAG24448.1; -; Genomic_DNA.
EMBL; AF306781; AAG24449.1; -; Genomic_DNA.
EMBL; AF306782; AAG24450.1; -; Genomic_DNA.
EMBL; AF306783; AAG24451.1; -; Genomic_DNA.
EMBL; AF268967; AAF86457.1; -; Genomic_DNA.
EMBL; AF065404; AAD32414.1; -; Genomic_DNA.
EMBL; AE011190; AAM26109.1; -; Genomic_DNA.
EMBL; AE017336; AAT28905.2; -; Genomic_DNA.
EMBL; AJ413936; CAC93934.1; -; Genomic_DNA.
EMBL; AJ413937; CAC93935.1; -; Genomic_DNA.
EMBL; AB125961; BAD14937.1; -; Genomic_DNA.
PIR; I39934; I39934.
RefSeq; NP_052806.1; NC_001496.1.
RefSeq; WP_000746486.1; NZ_MVKJ01000025.1.
RefSeq; WP_000746487.1; NZ_MVKE01000022.1.
RefSeq; WP_000746488.1; NZ_LGIF01000016.1.
PDB; 1ACC; X-ray; 2.10 A; A=30-764.
PDB; 1T6B; X-ray; 2.50 A; X=30-764.
PDB; 1TX5; Model; -; C=30-764.
PDB; 1TZN; X-ray; 4.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/O=203-764.
PDB; 1TZO; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/O=203-764.
PDB; 1V36; Model; -; A/B/C/D/E/F/G=197-764.
PDB; 3ETB; X-ray; 3.80 A; J/K/L/M=621-764.
PDB; 3INO; X-ray; 1.95 A; A/B=624-764.
PDB; 3J9C; EM; 2.90 A; A=203-764.
PDB; 3KWV; X-ray; 3.10 A; A/B/D/E=197-764.
PDB; 3MHZ; X-ray; 1.70 A; A=30-764.
PDB; 3Q8A; X-ray; 3.13 A; A=30-764.
PDB; 3Q8B; X-ray; 2.00 A; A=30-764.
PDB; 3Q8C; X-ray; 2.85 A; A=30-764.
PDB; 3Q8E; X-ray; 2.10 A; A=30-764.
PDB; 3Q8F; X-ray; 2.10 A; A=30-764.
PDB; 3TEW; X-ray; 1.45 A; A=30-764.
PDB; 3TEX; X-ray; 1.70 A; A=30-764.
PDB; 3TEY; X-ray; 2.12 A; A=30-764.
PDB; 3TEZ; X-ray; 1.83 A; A=30-764.
PDB; 4EE2; X-ray; 1.91 A; A=30-764.
PDB; 4H2A; X-ray; 1.62 A; A=30-764.
PDB; 4NAM; X-ray; 1.70 A; A=30-764.
PDB; 5FR3; X-ray; 1.94 A; A=43-764.
PDBsum; 1ACC; -.
PDBsum; 1T6B; -.
PDBsum; 1TX5; -.
PDBsum; 1TZN; -.
PDBsum; 1TZO; -.
PDBsum; 1V36; -.
PDBsum; 3ETB; -.
PDBsum; 3INO; -.
PDBsum; 3J9C; -.
PDBsum; 3KWV; -.
PDBsum; 3MHZ; -.
PDBsum; 3Q8A; -.
PDBsum; 3Q8B; -.
PDBsum; 3Q8C; -.
PDBsum; 3Q8E; -.
PDBsum; 3Q8F; -.
PDBsum; 3TEW; -.
PDBsum; 3TEX; -.
PDBsum; 3TEY; -.
PDBsum; 3TEZ; -.
PDBsum; 4EE2; -.
PDBsum; 4H2A; -.
PDBsum; 4NAM; -.
PDBsum; 5FR3; -.
ProteinModelPortal; P13423; -.
SMR; P13423; -.
DIP; DIP-29841N; -.
IntAct; P13423; 15.
MINT; MINT-7014733; -.
BindingDB; P13423; -.
ChEMBL; CHEMBL5352; -.
DrugBank; DB09057; Anthrax immune globulin human.
DrugBank; DB08902; Raxibacumab.
TCDB; 1.C.42.1.1; the channel-forming bacillus anthracis protective antigen (bapa) family.
EnsemblBacteria; AAM26109; AAM26109; BX_A0164.
EnsemblBacteria; AAT28905; AAT28905; GBAA_pXO1_0164.
GeneID; 3361714; -.
KEGG; bar:GBAA_pXO1_0164; -.
HOGENOM; HOG000034566; -.
KO; K11030; -.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
EvolutionaryTrace; P13423; -.
PMAP-CutDB; P13423; -.
PRO; PR:P13423; -.
Proteomes; UP000000594; Plasmid pXO1.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0010629; P:negative regulation of gene expression; IGI:UniProtKB.
GO; GO:0043409; P:negative regulation of MAPK cascade; IGI:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IGI:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:UniProtKB.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0044533; P:positive regulation of apoptotic process in other organism; IGI:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0035897; P:proteolysis in other organism; IGI:UniProtKB.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; IGI:UniProtKB.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IGI:UniProtKB.
Gene3D; 2.60.120.240; -; 1.
InterPro; IPR003896; Bacterial_exotoxin_B.
InterPro; IPR035331; Binary_toxB_3.
InterPro; IPR011658; PA14_dom.
InterPro; IPR035088; PA_Ca-bd.
InterPro; IPR027439; PA_heptamer_dom.
Pfam; PF03495; Binary_toxB; 1.
Pfam; PF17475; Binary_toxB_2; 1.
Pfam; PF17476; Binary_toxB_3; 1.
Pfam; PF07691; PA14; 1.
PRINTS; PR01391; BINARYTOXINB.
SMART; SM00758; PA14; 1.
PROSITE; PS51820; PA14; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cleavage on pair of basic residues;
Complete proteome; Metal-binding; Plasmid; Reference proteome;
Secreted; Signal; Toxin; Virulence.
SIGNAL 1 29
CHAIN 30 764 Protective antigen.
/FTId=PRO_0000021996.
CHAIN 30 196 Protective antigen PA-20.
/FTId=PRO_0000021997.
CHAIN 197 764 Protective antigen PA-63.
/FTId=PRO_0000021998.
DOMAIN 43 179 PA14. {ECO:0000255|PROSITE-
ProRule:PRU01164}.
REGION 30 287 Domain 1, calcium-binding; LF and EF
binding sites.
REGION 288 516 Domain 2, membrane insertion and
heptamerization.
REGION 517 624 Domain 3, heptamerization.
REGION 625 764 Domain 4, binding to the receptor.
METAL 206 206 Calcium.
METAL 208 208 Calcium.
METAL 210 210 Calcium.
METAL 217 217 Calcium.
SITE 196 197 Cleavage; by furin.
SITE 343 344 Cleavage; by chymotrypsin; required for
translocation of LF and EF.
SITE 712 712 Essential for binding to cell receptor.
VARIANT 295 295 M -> I (in strain: PAI).
VARIANT 392 392 N -> D (in strain: PAI).
VARIANT 560 560 F -> L (in Sverdlovsk sample).
VARIANT 565 565 P -> S (in strain: BA1024).
VARIANT 600 600 A -> V (in strain: BA1024, V770-NP1-R,
Carbosap and Ferrara).
MUTAGEN 213 213 P->A: Decrease in the ability to bind to
LF and partially toxic at high
concentrations.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 216 216 L->A: Decrease in the ability to bind to
LF and partially toxic at high
concentrations.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 231 231 F->A: Loss of ability to bind to LF and
completely nontoxic.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 232 232 L->A: Loss of ability to bind to LF and
completely nontoxic.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 234 234 P->A: Loss of ability to bind to LF and
completely nontoxic.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 236 236 I->A: Loss of ability to bind to LF and
completely nontoxic.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 239 239 I->A: Decrease in the ability to bind to
LF and partially toxic at high
concentrations.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 255 255 W->A: No effect on LF-binding ability and
as toxic as the wild-type.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 265 265 F->A: No effect on LF-binding ability and
as toxic as the wild-type.
{ECO:0000269|PubMed:12117959}.
MUTAGEN 289 289 P->A: Reduced toxicity in combination
with lethal factor. Decreased membrane
insertion and translocation of LF.
{ECO:0000269|PubMed:11356563}.
MUTAGEN 342 344 FFD->AAA: Decrease in toxicity probably
due to slow translocation of LF.
{ECO:0000269|PubMed:10085028}.
MUTAGEN 342 343 Missing: Loss of toxicity probably due to
loss of capability to translocate LF.
{ECO:0000269|PubMed:7961869}.
MUTAGEN 342 342 F->C: Loss of toxicity probably due to
loss of capability to translocate LF.
{ECO:0000269|PubMed:10085028}.
MUTAGEN 344 344 D->A: Decrease in toxicity probably due
to slow translocation of LF.
{ECO:0000269|PubMed:7961869}.
MUTAGEN 375 375 W->A: Loss of toxicity probably due to
faulty membrane insertion or
translocation of LF/EF into the cytosol.
{ECO:0000269|PubMed:11178978}.
MUTAGEN 379 379 M->A: No effect.
{ECO:0000269|PubMed:11178978}.
MUTAGEN 381 381 L->A: Loss of toxicity probably due to
faulty membrane insertion or
translocation of LF/EF into the cytosol.
{ECO:0000269|PubMed:11178978}.
MUTAGEN 393 393 I->C: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:14623961}.
MUTAGEN 409 409 T->C: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:14623961}.
MUTAGEN 411 411 S->C: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:14623961}.
MUTAGEN 422 422 T->C: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:14623961}.
MUTAGEN 426 426 K->A,D: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:11113126,
ECO:0000269|PubMed:14623961}.
MUTAGEN 428 428 N->C: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:14623961}.
MUTAGEN 440 440 Y->C: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:14623961}.
MUTAGEN 451 451 N->C: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:14623961}.
MUTAGEN 454 454 D->A,K: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:11113126,
ECO:0000269|PubMed:14623961}.
MUTAGEN 456 456 F->A: Loss of capability to undergo
conformational changes that lead to pore
formation and translocation.
{ECO:0000269|PubMed:11113126,
ECO:0000269|PubMed:14623961}.
MUTAGEN 512 512 Q->A: Loss of heptamerization capability.
{ECO:0000269|PubMed:11222612}.
MUTAGEN 541 541 D->A: Loss of heptamerization capability.
{ECO:0000269|PubMed:11222612}.
MUTAGEN 543 543 L->A: Decrease in heptamerization
capability.
{ECO:0000269|PubMed:11222612}.
MUTAGEN 581 581 F->A: Loss of toxicity due to defective
oligomerization.
{ECO:0000269|PubMed:11554763}.
MUTAGEN 583 583 F->A: Decrease in toxicity due to
defective oligomerization.
{ECO:0000269|PubMed:11554763}.
MUTAGEN 591 591 I->A: Loss of toxicity due to defective
oligomerization.
{ECO:0000269|PubMed:11554763}.
MUTAGEN 595 595 L->A: Loss of toxicity due to defective
oligomerization.
{ECO:0000269|PubMed:11554763}.
MUTAGEN 603 603 I->A: Loss of toxicity due to defective
oligomerization.
{ECO:0000269|PubMed:11554763}.
MUTAGEN 621 621 R->A: No effect.
{ECO:0000269|PubMed:11222612}.
MUTAGEN 686 686 N->A: Decrease in toxicity due to
decrease in cell binding.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 708 708 K->A: No effect on toxicity.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 709 709 K->A: Slight decrease in toxicity.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 710 710 Y->A: Great decrease in toxicity due to
decrease in cell binding.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 711 711 N->A: Loss of toxicity due to decrease in
cell binding.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 712 712 D->A: Loss of toxicity due to decrease in
cell binding.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 713 713 K->A: No effect on toxicity.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 714 714 L->A: No effect on toxicity.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 715 715 P->A: Great decrease in toxicity due to
decrease in cell binding.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 716 716 L->A: Decrease in toxicity due to
decrease in cell binding.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 717 717 Y->A: No effect on toxicity.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 718 718 I->A: Decrease in toxicity due to
decrease in cell binding.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 719 719 S->A: No effect on toxicity.
{ECO:0000269|PubMed:10085028}.
MUTAGEN 720 720 N->A: No effect on toxicity.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 721 721 P->A: No effect on toxicity.
{ECO:0000269|PubMed:12771151}.
MUTAGEN 722 722 N->A: No effect on toxicity.
{ECO:0000269|PubMed:12771151}.
CONFLICT 314 314 Q -> E (in Ref. 1; AAA22637).
{ECO:0000305}.
HELIX 41 44 {ECO:0000244|PDB:4H2A}.
STRAND 47 55 {ECO:0000244|PDB:3TEW}.
STRAND 60 71 {ECO:0000244|PDB:3TEW}.
HELIX 76 78 {ECO:0000244|PDB:3TEW}.
HELIX 84 86 {ECO:0000244|PDB:3TEW}.
STRAND 91 99 {ECO:0000244|PDB:3TEW}.
STRAND 104 110 {ECO:0000244|PDB:3TEW}.
HELIX 113 115 {ECO:0000244|PDB:3TEW}.
STRAND 116 120 {ECO:0000244|PDB:3TEW}.
STRAND 123 129 {ECO:0000244|PDB:3TEW}.
STRAND 135 137 {ECO:0000244|PDB:3TEW}.
STRAND 142 150 {ECO:0000244|PDB:3TEW}.
STRAND 155 159 {ECO:0000244|PDB:3TEW}.
STRAND 162 166 {ECO:0000244|PDB:3TEW}.
STRAND 168 170 {ECO:0000244|PDB:1ACC}.
STRAND 172 174 {ECO:0000244|PDB:3TEW}.
HELIX 177 179 {ECO:0000244|PDB:3TEW}.
STRAND 186 188 {ECO:0000244|PDB:3TEW}.
STRAND 191 193 {ECO:0000244|PDB:4H2A}.
STRAND 199 201 {ECO:0000244|PDB:3TEW}.
STRAND 210 212 {ECO:0000244|PDB:3TEW}.
HELIX 214 219 {ECO:0000244|PDB:3TEW}.
STRAND 221 225 {ECO:0000244|PDB:3TEW}.
STRAND 230 234 {ECO:0000244|PDB:3TEW}.
HELIX 237 240 {ECO:0000244|PDB:3TEW}.
TURN 241 244 {ECO:0000244|PDB:3TEW}.
STRAND 255 258 {ECO:0000244|PDB:3Q8A}.
STRAND 259 262 {ECO:0000244|PDB:3TEW}.
HELIX 264 269 {ECO:0000244|PDB:3TEW}.
HELIX 278 281 {ECO:0000244|PDB:3TEW}.
STRAND 291 302 {ECO:0000244|PDB:3TEW}.
STRAND 318 326 {ECO:0000244|PDB:3TEW}.
STRAND 331 340 {ECO:0000244|PDB:3J9C}.
STRAND 345 354 {ECO:0000244|PDB:3J9C}.
STRAND 357 363 {ECO:0000244|PDB:3TEW}.
STRAND 369 371 {ECO:0000244|PDB:3TEW}.
HELIX 375 379 {ECO:0000244|PDB:3TEW}.
STRAND 383 385 {ECO:0000244|PDB:3J9C}.
STRAND 386 397 {ECO:0000244|PDB:3TEW}.
STRAND 399 401 {ECO:0000244|PDB:3TEW}.
STRAND 403 405 {ECO:0000244|PDB:4EE2}.
STRAND 410 414 {ECO:0000244|PDB:3TEW}.
TURN 415 417 {ECO:0000244|PDB:3TEW}.
STRAND 418 423 {ECO:0000244|PDB:3TEW}.
TURN 427 429 {ECO:0000244|PDB:3J9C}.
STRAND 438 441 {ECO:0000244|PDB:3TEW}.
STRAND 448 451 {ECO:0000244|PDB:3TEW}.
STRAND 456 458 {ECO:0000244|PDB:3KWV}.
STRAND 461 464 {ECO:0000244|PDB:3TEW}.
HELIX 465 474 {ECO:0000244|PDB:3TEW}.
STRAND 476 481 {ECO:0000244|PDB:3TEW}.
STRAND 487 492 {ECO:0000244|PDB:3TEW}.
TURN 493 496 {ECO:0000244|PDB:3TEW}.
STRAND 497 505 {ECO:0000244|PDB:3TEW}.
HELIX 506 508 {ECO:0000244|PDB:3TEW}.
HELIX 510 516 {ECO:0000244|PDB:3TEW}.
STRAND 517 522 {ECO:0000244|PDB:3TEW}.
TURN 524 527 {ECO:0000244|PDB:3TEW}.
STRAND 530 535 {ECO:0000244|PDB:3TEW}.
HELIX 542 546 {ECO:0000244|PDB:3TEW}.
HELIX 552 560 {ECO:0000244|PDB:3TEW}.
STRAND 565 568 {ECO:0000244|PDB:3MHZ}.
HELIX 576 578 {ECO:0000244|PDB:3TEW}.
STRAND 579 583 {ECO:0000244|PDB:3TEW}.
HELIX 585 597 {ECO:0000244|PDB:3TEW}.
HELIX 603 605 {ECO:0000244|PDB:3TEW}.
TURN 607 609 {ECO:0000244|PDB:3TEW}.
STRAND 611 613 {ECO:0000244|PDB:3MHZ}.
STRAND 617 622 {ECO:0000244|PDB:3TEW}.
STRAND 625 627 {ECO:0000244|PDB:3TEW}.
STRAND 633 636 {ECO:0000244|PDB:3TEW}.
HELIX 638 644 {ECO:0000244|PDB:3TEW}.
STRAND 648 652 {ECO:0000244|PDB:3TEW}.
STRAND 655 658 {ECO:0000244|PDB:3TEW}.
HELIX 662 666 {ECO:0000244|PDB:3TEW}.
STRAND 668 676 {ECO:0000244|PDB:3TEW}.
STRAND 678 680 {ECO:0000244|PDB:3KWV}.
STRAND 682 684 {ECO:0000244|PDB:3TEW}.
HELIX 689 691 {ECO:0000244|PDB:4EE2}.
STRAND 695 697 {ECO:0000244|PDB:3TEW}.
TURN 699 701 {ECO:0000244|PDB:3KWV}.
STRAND 703 708 {ECO:0000244|PDB:3TEW}.
TURN 709 713 {ECO:0000244|PDB:3TEW}.
STRAND 723 731 {ECO:0000244|PDB:3TEW}.
HELIX 732 734 {ECO:0000244|PDB:3TEW}.
STRAND 741 743 {ECO:0000244|PDB:1ACC}.
STRAND 753 759 {ECO:0000244|PDB:3TEW}.
HELIX 760 763 {ECO:0000244|PDB:3TEW}.
SEQUENCE 764 AA; 85811 MW; 3AE1EFBF48FAA03F CRC64;
MKKRKVLIPL MALSTILVSS TGNLEVIQAE VKQENRLLNE SESSSQGLLG YYFSDLNFQA
PMVVTSSTTG DLSIPSSELE NIPSENQYFQ SAIWSGFIKV KKSDEYTFAT SADNHVTMWV
DDQEVINKAS NSNKIRLEKG RLYQIKIQYQ RENPTEKGLD FKLYWTDSQN KKEVISSDNL
QLPELKQKSS NSRKKRSTSA GPTVPDRDND GIPDSLEVEG YTVDVKNKRT FLSPWISNIH
EKKGLTKYKS SPEKWSTASD PYSDFEKVTG RIDKNVSPEA RHPLVAAYPI VHVDMENIIL
SKNEDQSTQN TDSQTRTISK NTSTSRTHTS EVHGNAEVHA SFFDIGGSVS AGFSNSNSST
VAIDHSLSLA GERTWAETMG LNTADTARLN ANIRYVNTGT APIYNVLPTT SLVLGKNQTL
ATIKAKENQL SQILAPNNYY PSKNLAPIAL NAQDDFSSTP ITMNYNQFLE LEKTKQLRLD
TDQVYGNIAT YNFENGRVRV DTGSNWSEVL PQIQETTARI IFNGKDLNLV ERRIAAVNPS
DPLETTKPDM TLKEALKIAF GFNEPNGNLQ YQGKDITEFD FNFDQQTSQN IKNQLAELNA
TNIYTVLDKI KLNAKMNILI RDKRFHYDRN NIAVGADESV VKEAHREVIN SSTEGLLLNI
DKDIRKILSG YIVEIEDTEG LKEVINDRYD MLNISSLRQD GKTFIDFKKY NDKLPLYISN
PNYKVNVYAV TKENTIINPS ENGDTSTNGI KKILIFSKKG YEIG


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