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Lethal factor (LF) (EC 3.4.24.83) (Anthrax lethal toxin endopeptidase component)

 LEF_BACAN               Reviewed;         809 AA.
P15917; Q8KYJ6; Q933F6;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
05-JUL-2017, entry version 164.
RecName: Full=Lethal factor;
Short=LF;
EC=3.4.24.83;
AltName: Full=Anthrax lethal toxin endopeptidase component;
Flags: Precursor;
Name=lef; OrderedLocusNames=pXO1-107, BXA0172, GBAA_pXO1_0172;
Bacillus anthracis.
Plasmid pXO1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1392;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-49.
PubMed=2509294; DOI=10.1016/0378-1119(89)90335-1;
Bragg T.S., Robertson D.L.;
"Nucleotide sequence and analysis of the lethal factor gene (lef) from
Bacillus anthracis.";
Gene 81:45-54(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lowe J.;
"A comparison of Bacillus anthracis sequences.";
Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
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).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-809.
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).
[7]
FUNCTION.
PubMed=9563949; DOI=10.1126/science.280.5364.734;
Duesbery N.S., Webb C.P., Leppla S.H., Gordon V.M., Klimpel K.R.,
Copeland T.D., Ahn N.G., Oskarsson M.K., Fukasawa K., Paull K.D.,
Vande Woude G.F.;
"Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal
factor.";
Science 280:734-737(1998).
[8]
FUNCTION.
PubMed=9703991; DOI=10.1006/bbrc.1998.9040;
Vitale G., Pellizzari R., Recchi C., Napolitani G., Mock M.,
Montecucco C.;
"Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces
tyrosine/threonine phosphorylation of MAPKs in cultured macrophages.";
Biochem. Biophys. Res. Commun. 248:706-711(1998).
[9]
FUNCTION.
PubMed=10475971; DOI=10.1046/j.1365-2672.1999.00892.x;
Duesbery N.S., Vande Woude G.F.;
"Anthrax lethal factor causes proteolytic inactivation of mitogen-
activated protein kinase kinase.";
J. Appl. Microbiol. 87:289-293(1999).
[10]
FUNCTION.
PubMed=11104681; DOI=10.1042/bj3520739;
Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.;
"Susceptibility of mitogen-activated protein kinase kinase family
members to proteolysis by anthrax lethal factor.";
Biochem. J. 352:739-745(2000).
[11]
FUNCTION.
PubMed=10338520;
Tang G., Leppla S.H.;
"Proteasome activity is required for anthrax lethal toxin to kill
macrophages.";
Infect. Immun. 67:3055-3060(1999).
[12]
CHARACTERIZATION.
PubMed=8942659; DOI=10.1021/bi961518b;
Wang X.-M., Mock M., Ruysschaert J.-M., Cabiaux V.;
"Secondary structure of anthrax lethal toxin proteins and their
interaction with large unilamellar vesicles: a Fourier-transform
infrared spectroscopy approach.";
Biochemistry 35:14939-14946(1996).
[13]
ZINC-BINDING.
PubMed=7851740; DOI=10.1111/j.1574-6968.1994.tb07306.x;
Kochi S.K., Schiavo G., Mock M., Montecucco C.;
"Zinc content of the Bacillus anthracis lethal factor.";
FEMS Microbiol. Lett. 124:343-348(1994).
[14]
REGULATION OF TOXIN EXPRESSION.
STRAIN=Sterne;
PubMed=8051039; DOI=10.1128/jb.176.16.5188-5192.1994;
Sirard J.-C., Mock M., Fouet A.;
"The three Bacillus anthracis toxin genes are coordinately regulated
by bicarbonate and temperature.";
J. Bacteriol. 176:5188-5192(1994).
[15]
MUTAGENESIS OF HIS-719; GLU-720 AND HIS-723, AND ACTIVE SITE.
STRAIN=Sterne;
PubMed=9573135;
Hammond S.E., Hanna P.C.;
"Lethal factor active-site mutations affect catalytic activity in
vitro.";
Infect. Immun. 66:2374-2378(1998).
[16]
MUTAGENESIS OF VAL-180; TYR-181; TYR-182; GLU-183; ILE-184; GLY-185
AND LYS-186.
STRAIN=Sterne;
PubMed=11162493; DOI=10.1006/bbrc.2000.4099;
Gupta P., Singh A., Chauhan V., Bhatnagar R.;
"Involvement of residues 147VYYEIGK153 in binding of lethal factor to
protective antigen of Bacillus anthracis.";
Biochem. Biophys. Res. Commun. 280:158-163(2001).
[17]
MUTAGENESIS OF ASP-220; LEU-221; LEU-222 AND PHE-223.
STRAIN=Sterne;
PubMed=12113932; DOI=10.1111/j.1574-6968.2002.tb11264.x;
Singh A., Chauhan V., Sodhi A., Bhatnagar R.;
"Asp 187 and Phe 190 residues in lethal factor are required for the
expression of anthrax lethal toxin activity.";
FEMS Microbiol. Lett. 212:183-186(2002).
[18]
REVIEW.
PubMed=11595637; DOI=10.1016/S0041-0101(01)00161-1;
Brossier F., Mock M.;
"Toxins of Bacillus anthracis.";
Toxicon 39:1747-1755(2001).
[19]
FUNCTION, MUTAGENESIS OF GLU-720, AND ACTIVE SITE.
PubMed=19651869; DOI=10.1128/IAI.00276-09;
Liao K.C., Mogridge J.;
"Expression of Nlrp1b inflammasome components in human fibroblasts
confers susceptibility to anthrax lethal toxin.";
Infect. Immun. 77:4455-4462(2009).
[20]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
MAP2K2, AND COFACTOR.
PubMed=11700563; DOI=10.1038/n35101998;
Pannifer A.D., Wong T.Y., Schwarzenbacher R., Renatus M., Petosa C.,
Bienkowska J., Lacy D.B., Collier R.J., Park S., Leppla S.H.,
Hanna P.C., Liddington R.C.;
"Crystal structure of the anthrax lethal factor.";
Nature 414:229-233(2001).
[21]
X-RAY CRYSTALLOGRAPHY (3.52 ANGSTROMS) OF 34-809 IN COMPLEX WITH ZINC
IONS AND PEPTIDE SUBSTRATE ANALOG, AND COFACTOR.
PubMed=14718924; DOI=10.1038/nsmb708;
Turk B.E., Wong T.Y., Schwarzenbacher R., Jarrell E.T., Leppla S.H.,
Collier R.J., Liddington R.C., Cantley L.C.;
"The structural basis for substrate and inhibitor selectivity of the
anthrax lethal factor.";
Nat. Struct. Mol. Biol. 11:60-66(2004).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 297-809 IN COMPLEX WITH ZINC
IONS AND PROTEASE INHIBITOR, AND COFACTOR.
PubMed=15911756; DOI=10.1073/pnas.0502159102;
Shoop W.L., Xiong Y., Wiltsie J., Woods A., Guo J., Pivnichny J.V.,
Felcetto T., Michael B.F., Bansal A., Cummings R.T., Cunningham B.R.,
Friedlander A.M., Douglas C.M., Patel S.B., Wisniewski D., Scapin G.,
Salowe S.P., Zaller D.M., Chapman K.T., Scolnick E.M., Schmatz D.M.,
Bartizal K., MacCoss M., Hermes J.D.;
"Anthrax lethal factor inhibition.";
Proc. Natl. Acad. Sci. U.S.A. 102:7958-7963(2005).
-!- FUNCTION: One of the three proteins composing the anthrax toxin,
the agent which infects many mammalian species and that may cause
death. LF is the lethal factor that, when associated with PA,
causes death. LF is not toxic by itself. It is a protease that
cleaves the N-terminal of most dual specificity mitogen-activated
protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5).
Cleavage invariably occurs within the N-terminal proline-rich
region preceding the kinase domain, thus disrupting a sequence
involved in directing specific protein-protein interactions
necessary for the assembly of signaling complexes. There may be
other cytosolic targets of LF involved in cytotoxicity. The
proteasome may mediate a toxic process initiated by LF in the cell
cytosol involving degradation of unidentified molecules that are
essential for macrophage homeostasis. This is an early step in
LeTx intoxication, but it is downstream of the cleavage by LF of
MEK1 or other putative substrates. Also cleaves mouse Nlrp1b
allele 1, leading to NLRP1 inflammasome activation, IL1B release
and eventually host inflammatory response (PubMed:19651869).
{ECO:0000269|PubMed:10338520, ECO:0000269|PubMed:10475971,
ECO:0000269|PubMed:11104681, ECO:0000269|PubMed:19651869,
ECO:0000269|PubMed:9563949, ECO:0000269|PubMed:9703991}.
-!- CATALYTIC ACTIVITY: Preferred amino acids around the cleavage site
can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H
denotes a hydrophobic amino acid, and x is any amino acid. The
only known protein substrates are mitogen-activated protein (MAP)
kinase kinases.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11700563,
ECO:0000269|PubMed:14718924, ECO:0000269|PubMed:15911756,
ECO:0000269|PubMed:7851740};
Note=Binds 1 zinc ion per subunit.;
-!- 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).
{ECO:0000269|PubMed:11700563, ECO:0000269|PubMed:14718924,
ECO:0000269|PubMed:15911756}.
-!- INTERACTION:
P13423:pagA; NbExp=5; IntAct=EBI-456923, EBI-456868;
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: Positively transcriptionally regulated by AtxA, which,
in turn, is induced by bicarbonate and high temperatures (37
degrees Celsius).
-!- DOMAIN: It comprises four domains: domain I binds the membrane-
translocating component (PA); domains II, III and IV together
create a long deep groove that holds the 16-residue N-terminal
tail of MAPKK before cleavage. Domain IV contains the catalytic
center.
-!- DOMAIN: The PA-binding region is found in both B.anthracis EF and
LF.
-!- MISCELLANEOUS: LF binds to the heptamer formed by cleaved PA on
the host cell membrane. This step is followed by internalization
of the heterooligomeric complex by receptor-mediated endocytosis.
LeTx requires passage through an acidic vesicle for activity; at
acidic pH, as the pore is inserted into the membrane, LF is
translocated and reaches its cytosolic targets. LF is probably
directly involved in its routing, by interacting with the lipid
membrane. This interaction could involve a conformational change
of LF and/or an oligomerization of the protein. LF may have the
capability of partially unfolding in order to cross the membrane.
-!- SIMILARITY: Belongs to the peptidase M34 family. {ECO:0000305}.
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EMBL; M29081; AAA79216.1; -; Genomic_DNA.
EMBL; M30210; AAA22569.1; -; Genomic_DNA.
EMBL; AF065404; AAD32411.1; -; Genomic_DNA.
EMBL; AE011190; AAM26117.1; -; Genomic_DNA.
EMBL; AE017336; AAT28913.2; -; Genomic_DNA.
EMBL; AJ413934; CAC93932.1; -; Genomic_DNA.
EMBL; AJ413935; CAC93933.1; -; Genomic_DNA.
PIR; JQ0032; JQ0032.
RefSeq; NP_052803.1; NC_001496.1.
RefSeq; WP_001022097.1; NZ_MVKJ01000025.1.
RefSeq; WP_010890024.1; NZ_JTAE01000006.1.
PDB; 1J7N; X-ray; 2.30 A; A/B=34-809.
PDB; 1JKY; X-ray; 3.90 A; A=34-809.
PDB; 1PWP; X-ray; 2.90 A; A/B=34-809.
PDB; 1PWQ; X-ray; 3.52 A; A/B=34-809.
PDB; 1PWU; X-ray; 2.70 A; A/B=34-809.
PDB; 1PWV; X-ray; 2.85 A; A/B=34-809.
PDB; 1PWW; X-ray; 2.80 A; A/B=34-809.
PDB; 1YQY; X-ray; 2.30 A; A=297-809.
PDB; 1ZXV; X-ray; 2.67 A; A/B=34-809.
PDB; 2L0R; NMR; -; A=705-809.
PDB; 3KWV; X-ray; 3.10 A; C/F=34-296.
PDB; 4DV8; X-ray; 1.63 A; A=296-809.
PDB; 4PKQ; X-ray; 2.20 A; A=298-809.
PDB; 4PKR; X-ray; 2.20 A; A=298-809.
PDB; 4PKS; X-ray; 2.30 A; A=298-809.
PDB; 4PKT; X-ray; 2.40 A; A=298-809.
PDB; 4PKU; X-ray; 2.40 A; A=298-809.
PDB; 4PKV; X-ray; 2.50 A; A=298-809.
PDB; 4PKW; X-ray; 1.75 A; A=298-809.
PDB; 4WF6; X-ray; 2.65 A; A=298-809.
PDB; 4XM6; X-ray; 2.35 A; A=298-809.
PDB; 4XM7; X-ray; 2.70 A; A=298-809.
PDB; 4XM8; X-ray; 2.70 A; A=298-809.
PDB; 5D1S; X-ray; 2.10 A; A=298-809.
PDB; 5D1T; X-ray; 2.20 A; A=298-809.
PDB; 5D1U; X-ray; 2.85 A; A=298-809.
PDBsum; 1J7N; -.
PDBsum; 1JKY; -.
PDBsum; 1PWP; -.
PDBsum; 1PWQ; -.
PDBsum; 1PWU; -.
PDBsum; 1PWV; -.
PDBsum; 1PWW; -.
PDBsum; 1YQY; -.
PDBsum; 1ZXV; -.
PDBsum; 2L0R; -.
PDBsum; 3KWV; -.
PDBsum; 4DV8; -.
PDBsum; 4PKQ; -.
PDBsum; 4PKR; -.
PDBsum; 4PKS; -.
PDBsum; 4PKT; -.
PDBsum; 4PKU; -.
PDBsum; 4PKV; -.
PDBsum; 4PKW; -.
PDBsum; 4WF6; -.
PDBsum; 4XM6; -.
PDBsum; 4XM7; -.
PDBsum; 4XM8; -.
PDBsum; 5D1S; -.
PDBsum; 5D1T; -.
PDBsum; 5D1U; -.
ProteinModelPortal; P15917; -.
SMR; P15917; -.
DIP; DIP-29871N; -.
IntAct; P15917; 1.
MINT; MINT-7014731; -.
BindingDB; P15917; -.
ChEMBL; CHEMBL4372; -.
DrugBank; DB07290; (2R)-2-{[(4-FLUORO-3-METHYLPHENYL)SULFONYL]AMINO}-N-HYDROXY-2-TETRAHYDRO-2H-PYRAN-4-YLACETAMIDE.
DrugBank; DB08177; (E)-3-(5((5-(4-CHLOROPHENYL)FURAN-2-YL)METHYLENE)-4-OXO-2-THIOXOTHIAZOLIDIN-3-YL)PROPANOIC ACID.
DrugBank; DB02255; GM6001.
DrugBank; DB01883; N-(Sulfanylacetyl)Tyrosylprolylmethioninamide.
MEROPS; M34.001; -.
EnsemblBacteria; AAM26117; AAM26117; BX_A0172.
EnsemblBacteria; AAT28913; AAT28913; GBAA_pXO1_0172.
GeneID; 3361711; -.
KEGG; bar:GBAA_pXO1_0172; -.
HOGENOM; HOG000034565; -.
KO; K08645; -.
BRENDA; 3.4.24.83; 634.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
EvolutionaryTrace; P15917; -.
PRO; PR:P15917; -.
Proteomes; UP000000594; Plasmid pXO1.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; EXP:Reactome.
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; IEP:CACAO.
GO; GO:0044533; P:positive regulation of apoptotic process in other organism; IGI:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:CACAO.
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; 3.40.390.10; -; 2.
InterPro; IPR015239; Anthrax_tox_lethal-fac_cen.
InterPro; IPR003541; Anthrax_toxin_lethal/edema.
InterPro; IPR014781; Anthrax_toxin_lethal/edema_N/C.
InterPro; IPR024079; MetalloPept_cat_dom.
Pfam; PF09156; Anthrax-tox_M; 1.
Pfam; PF07737; ATLF; 2.
PRINTS; PR01392; ANTHRAXTOXNA.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Hydrolase;
Metal-binding; Metalloprotease; Plasmid; Protease; Reference proteome;
Repeat; Secreted; Signal; Toxin; Virulence; Zinc.
SIGNAL 1 33 {ECO:0000269|PubMed:2509294}.
CHAIN 34 809 Lethal factor.
/FTId=PRO_0000029233.
REPEAT 315 333 1.
REPEAT 342 357 2.
REPEAT 360 378 3.
REPEAT 380 397 4.
REPEAT 399 416 5.
REGION 34 293 PA-binding region. {ECO:0000255}.
REGION 60 295 I; PA-binding region. {ECO:0000255}.
REGION 296 330 IIA.
REGION 315 416 5 X approximate repeats.
REGION 336 416 III.
REGION 420 583 IIB.
REGION 585 809 IV.
ACT_SITE 720 720 {ECO:0000269|PubMed:19651869,
ECO:0000269|PubMed:9573135}.
METAL 719 719 Zinc; catalytic.
{ECO:0000269|PubMed:11700563,
ECO:0000269|PubMed:14718924,
ECO:0000269|PubMed:15911756}.
METAL 723 723 Zinc; catalytic.
{ECO:0000269|PubMed:11700563,
ECO:0000269|PubMed:14718924,
ECO:0000269|PubMed:15911756}.
METAL 768 768 Zinc; catalytic.
{ECO:0000269|PubMed:11700563,
ECO:0000269|PubMed:14718924,
ECO:0000269|PubMed:15911756}.
VARIANT 299 299 A -> S (in strain: Sterne).
MUTAGEN 180 180 V->A: No effect on PA-binding ability.
{ECO:0000269|PubMed:11162493}.
MUTAGEN 181 181 Y->A: Loss of ability to bind to PA.
{ECO:0000269|PubMed:11162493}.
MUTAGEN 182 182 Y->A: Loss of ability to bind to PA.
{ECO:0000269|PubMed:11162493}.
MUTAGEN 183 183 E->A: No effect on PA-binding ability.
{ECO:0000269|PubMed:11162493}.
MUTAGEN 184 184 I->A: Loss of ability to bind to PA.
{ECO:0000269|PubMed:11162493}.
MUTAGEN 185 185 G->A: No effect on PA-binding ability.
{ECO:0000269|PubMed:11162493}.
MUTAGEN 186 186 K->A: Loss of ability to bind to PA.
{ECO:0000269|PubMed:11162493}.
MUTAGEN 220 220 D->A: Loss of ability to bind to PA and
loss of toxicity.
{ECO:0000269|PubMed:12113932}.
MUTAGEN 221 221 L->A: No effect on PA-binding ability and
fully toxic.
{ECO:0000269|PubMed:12113932}.
MUTAGEN 222 222 L->A: No effect on PA-binding ability and
fully toxic.
{ECO:0000269|PubMed:12113932}.
MUTAGEN 223 223 F->A: Loss of ability to bind to PA and
non-toxic. {ECO:0000269|PubMed:12113932}.
MUTAGEN 719 719 H->A: Loss of activity and zinc binding.
{ECO:0000269|PubMed:9573135}.
MUTAGEN 720 720 E->C,D: Loss of activity. No effect on
zinc binding.
{ECO:0000269|PubMed:19651869,
ECO:0000269|PubMed:9573135}.
MUTAGEN 723 723 H->A: Loss of activity and zinc binding.
{ECO:0000269|PubMed:9573135}.
TURN 62 65 {ECO:0000244|PDB:1J7N}.
HELIX 66 76 {ECO:0000244|PDB:1J7N}.
STRAND 77 80 {ECO:0000244|PDB:1J7N}.
HELIX 87 97 {ECO:0000244|PDB:1J7N}.
HELIX 101 109 {ECO:0000244|PDB:1J7N}.
STRAND 113 119 {ECO:0000244|PDB:1J7N}.
HELIX 121 123 {ECO:0000244|PDB:1J7N}.
HELIX 125 127 {ECO:0000244|PDB:1J7N}.
HELIX 132 135 {ECO:0000244|PDB:1J7N}.
STRAND 136 138 {ECO:0000244|PDB:1J7N}.
STRAND 144 146 {ECO:0000244|PDB:1J7N}.
HELIX 147 149 {ECO:0000244|PDB:1J7N}.
STRAND 151 155 {ECO:0000244|PDB:1J7N}.
STRAND 157 159 {ECO:0000244|PDB:1J7N}.
STRAND 161 165 {ECO:0000244|PDB:1J7N}.
TURN 170 172 {ECO:0000244|PDB:1J7N}.
HELIX 174 190 {ECO:0000244|PDB:1J7N}.
HELIX 193 196 {ECO:0000244|PDB:1J7N}.
HELIX 201 211 {ECO:0000244|PDB:1J7N}.
STRAND 213 216 {ECO:0000244|PDB:1J7N}.
HELIX 217 222 {ECO:0000244|PDB:1J7N}.
HELIX 225 228 {ECO:0000244|PDB:1J7N}.
HELIX 236 240 {ECO:0000244|PDB:1J7N}.
HELIX 243 258 {ECO:0000244|PDB:1J7N}.
HELIX 260 269 {ECO:0000244|PDB:1J7N}.
HELIX 271 282 {ECO:0000244|PDB:1J7N}.
HELIX 284 293 {ECO:0000244|PDB:1J7N}.
HELIX 300 310 {ECO:0000244|PDB:4DV8}.
HELIX 312 317 {ECO:0000244|PDB:4DV8}.
HELIX 320 330 {ECO:0000244|PDB:4DV8}.
HELIX 337 342 {ECO:0000244|PDB:4DV8}.
HELIX 346 354 {ECO:0000244|PDB:4DV8}.
HELIX 357 359 {ECO:0000244|PDB:4DV8}.
STRAND 361 363 {ECO:0000244|PDB:4PKW}.
HELIX 365 379 {ECO:0000244|PDB:4DV8}.
STRAND 381 383 {ECO:0000244|PDB:4PKR}.
HELIX 384 389 {ECO:0000244|PDB:4DV8}.
TURN 390 392 {ECO:0000244|PDB:5D1S}.
TURN 393 396 {ECO:0000244|PDB:4PKV}.
HELIX 403 412 {ECO:0000244|PDB:4DV8}.
HELIX 413 415 {ECO:0000244|PDB:4DV8}.
HELIX 421 428 {ECO:0000244|PDB:4DV8}.
STRAND 435 437 {ECO:0000244|PDB:4DV8}.
HELIX 439 455 {ECO:0000244|PDB:4DV8}.
STRAND 458 460 {ECO:0000244|PDB:1PWV}.
HELIX 461 464 {ECO:0000244|PDB:4DV8}.
TURN 465 467 {ECO:0000244|PDB:4DV8}.
STRAND 470 474 {ECO:0000244|PDB:4DV8}.
HELIX 476 478 {ECO:0000244|PDB:4DV8}.
HELIX 481 484 {ECO:0000244|PDB:4DV8}.
STRAND 486 488 {ECO:0000244|PDB:5D1T}.
HELIX 498 505 {ECO:0000244|PDB:4DV8}.
STRAND 510 515 {ECO:0000244|PDB:4DV8}.
STRAND 518 522 {ECO:0000244|PDB:4DV8}.
STRAND 532 537 {ECO:0000244|PDB:4DV8}.
STRAND 543 547 {ECO:0000244|PDB:4DV8}.
TURN 548 550 {ECO:0000244|PDB:4DV8}.
STRAND 551 554 {ECO:0000244|PDB:4DV8}.
STRAND 556 570 {ECO:0000244|PDB:4DV8}.
STRAND 573 583 {ECO:0000244|PDB:4DV8}.
HELIX 585 607 {ECO:0000244|PDB:4DV8}.
STRAND 616 619 {ECO:0000244|PDB:4DV8}.
HELIX 625 642 {ECO:0000244|PDB:4DV8}.
HELIX 645 657 {ECO:0000244|PDB:4DV8}.
STRAND 662 667 {ECO:0000244|PDB:4DV8}.
HELIX 669 671 {ECO:0000244|PDB:4DV8}.
HELIX 673 676 {ECO:0000244|PDB:4DV8}.
HELIX 682 684 {ECO:0000244|PDB:4DV8}.
STRAND 688 693 {ECO:0000244|PDB:4DV8}.
HELIX 694 696 {ECO:0000244|PDB:4DV8}.
STRAND 698 705 {ECO:0000244|PDB:4DV8}.
TURN 709 711 {ECO:0000244|PDB:2L0R}.
HELIX 713 733 {ECO:0000244|PDB:4DV8}.
STRAND 735 737 {ECO:0000244|PDB:4DV8}.
HELIX 741 743 {ECO:0000244|PDB:4DV8}.
HELIX 745 754 {ECO:0000244|PDB:4DV8}.
TURN 755 757 {ECO:0000244|PDB:4PKV}.
HELIX 761 763 {ECO:0000244|PDB:4DV8}.
HELIX 766 777 {ECO:0000244|PDB:4DV8}.
HELIX 782 791 {ECO:0000244|PDB:4DV8}.
HELIX 793 807 {ECO:0000244|PDB:4DV8}.
SEQUENCE 809 AA; 93770 MW; 2076B4D7277317EE CRC64;
MNIKKEFIKV ISMSCLVTAI TLSGPVFIPL VQGAGGHGDV GMHVKEKEKN KDENKRKDEE
RNKTQEEHLK EIMKHIVKIE VKGEEAVKKE AAEKLLEKVP SDVLEMYKAI GGKIYIVDGD
ITKHISLEAL SEDKKKIKDI YGKDALLHEH YVYAKEGYEP VLVIQSSEDY VENTEKALNV
YYEIGKILSR DILSKINQPY QKFLDVLNTI KNASDSDGQD LLFTNQLKEH PTDFSVEFLE
QNSNEVQEVF AKAFAYYIEP QHRDVLQLYA PEAFNYMDKF NEQEINLSLE ELKDQRMLAR
YEKWEKIKQH YQHWSDSLSE EGRGLLKKLQ IPIEPKKDDI IHSLSQEEKE LLKRIQIDSS
DFLSTEEKEF LKKLQIDIRD SLSEEEKELL NRIQVDSSNP LSEKEKEFLK KLKLDIQPYD
INQRLQDTGG LIDSPSINLD VRKQYKRDIQ NIDALLHQSI GSTLYNKIYL YENMNINNLT
ATLGADLVDS TDNTKINRGI FNEFKKNFKY SISSNYMIVD INERPALDNE RLKWRIQLSP
DTRAGYLENG KLILQRNIGL EIKDVQIIKQ SEKEYIRIDA KVVPKSKIDT KIQEAQLNIN
QEWNKALGLP KYTKLITFNV HNRYASNIVE SAYLILNEWK NNIQSDLIKK VTNYLVDGNG
RFVFTDITLP NIAEQYTHQD EIYEQVHSKG LYVPESRSIL LHGPSKGVEL RNDSEGFIHE
FGHAVDDYAG YLLDKNQSDL VTNSKKFIDI FKEEGSNLTS YGRTNEAEFF AEAFRLMHST
DHAERLKVQK NAPKTFQFIN DQIKFIINS


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