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Lys-gingipain W83 (EC 3.4.22.47) (Lysine specific cysteine protease) (Lysine-specific cysteine proteinase) (Porphypain) (PrtK48) [Cleaved into: Lys-gingipain catalytic subunit; 39 kDa adhesin (PrtK39); 15 kDa adhesin (PrtK15); 44 kDa adhesin (PrtK44)]

 KGP83_PORGN             Reviewed;        1732 AA.
Q51817; O07442; O52050;
13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 82.
RecName: Full=Lys-gingipain W83 {ECO:0000250|UniProtKB:B2RLK2, ECO:0000303|PubMed:15297553};
EC=3.4.22.47 {ECO:0000269|PubMed:9245829};
AltName: Full=Lysine specific cysteine protease {ECO:0000303|PubMed:9632563, ECO:0000312|EMBL:AAC26523.1};
AltName: Full=Lysine-specific cysteine proteinase {ECO:0000303|PubMed:10219167, ECO:0000312|EMBL:AAB60809.1};
AltName: Full=Porphypain {ECO:0000303|PubMed:8631659, ECO:0000312|EMBL:AAB06565.1};
AltName: Full=PrtK48 {ECO:0000303|PubMed:10219167};
Contains:
RecName: Full=Lys-gingipain catalytic subunit {ECO:0000250|UniProtKB:B2RLK2, ECO:0000303|PubMed:9245829};
Contains:
RecName: Full=39 kDa adhesin {ECO:0000303|PubMed:9245829};
AltName: Full=PrtK39 {ECO:0000303|PubMed:10219167};
Contains:
RecName: Full=15 kDa adhesin {ECO:0000303|PubMed:9245829};
AltName: Full=PrtK15 {ECO:0000303|PubMed:10219167};
Contains:
RecName: Full=44 kDa adhesin {ECO:0000303|PubMed:9245829};
AltName: Full=PrtK44 {ECO:0000303|PubMed:10219167};
Flags: Precursor;
Name=kgp {ECO:0000250|UniProtKB:B2RLK2};
Synonyms=prtK {ECO:0000312|EMBL:AAB60809.1},
prtP {ECO:0000303|PubMed:9632563, ECO:0000312|EMBL:AAB06565.1};
Porphyromonas gingivalis.
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
Porphyromonadaceae; Porphyromonas.
NCBI_TaxID=837;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB06565.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=W12 {ECO:0000312|EMBL:AAB06565.1};
PubMed=8631659; DOI=10.1128/jb.178.10.2734-2741.1996;
Barkocy-Gallagher G.A., Han N., Patti J.M., Whitlock J.,
Progulske-Fox A., Lantz M.S.;
"Analysis of the prtP gene encoding porphypain, a cysteine proteinase
of Porphyromonas gingivalis.";
J. Bacteriol. 178:2734-2741(1996).
[2] {ECO:0000312|EMBL:AAC26523.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC BAA-308 / W83 {ECO:0000312|EMBL:AAC26523.1};
PubMed=9632563;
Lewis J.P., Macrina F.L.;
"IS195, an insertion sequence-like element associated with protease
genes in Porphyromonas gingivalis.";
Infect. Immun. 66:3035-3042(1998).
[3] {ECO:0000305, ECO:0000312|EMBL:AAB60809.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 53978 / W50 {ECO:0000312|EMBL:AAB60809.1};
PubMed=10219167; DOI=10.1034/j.1399-302X.1999.140203.x;
Slakeski N., Cleal S.M., Bhogal P.S., Reynolds E.C.;
"Characterization of a Porphyromonas gingivalis gene prtK that encodes
a lysine-specific cysteine proteinase and three sequence-related
adhesins.";
Oral Microbiol. Immunol. 14:92-97(1999).
[4] {ECO:0000305}
PROTEIN SEQUENCE OF 229-245; 738-763; 1157-1180 AND 1292-1313,
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 53978 / W50 {ECO:0000269|PubMed:9245829};
PubMed=9245829; DOI=10.1099/00221287-143-7-2485;
Bhogal P.S., Slakeski N., Reynolds E.C.;
"A cell-associated protein complex of Porphyromonas gingivalis W50
composed of Arg- and Lys-specific cysteine proteinases and adhesins.";
Microbiology 143:2485-2495(1997).
[5] {ECO:0000305}
POLYMORPHISM.
PubMed=15297553; DOI=10.1128/JCM.42.8.3873-3876.2004;
Nadkarni M.A., Nguyen K.A., Chapple C.C., DeCarlo A.A., Jacques N.A.,
Hunter N.;
"Distribution of Porphyromonas gingivalis biotypes defined by alleles
of the kgp (Lys-gingipain) gene.";
J. Clin. Microbiol. 42:3873-3876(2004).
[6]
X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 1427-1602 IN COMPLEX WITH
CALCIUM, DOMAIN, AND FUNCTION.
STRAIN=ATCC BAA-308 / W83 {ECO:0000303|PubMed:21812842};
PubMed=21812842; DOI=10.1111/j.1365-2958.2011.07768.x;
Li N., Yun P., Jeffries C.M., Langley D., Gamsjaeger R., Church W.B.,
Hunter N., Collyer C.A.;
"The modular structure of haemagglutinin/adhesin regions in gingipains
of Porphyromonas gingivalis.";
Mol. Microbiol. 81:1358-1373(2011).
[7]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 982-1154 IN COMPLEX WITH
CALCIUM, AND FUNCTION.
STRAIN=ATCC BAA-308 / W83 {ECO:0000303|PubMed:24265933};
PubMed=24265933; DOI=10.1556/EuJMI.3.2013.3.2;
Ganuelas L.A., Li N., Yun P., Hunter N., Collyer C.A.;
"The lysine gingipain adhesin domains from Porphyromonas gingivalis
interact with erythrocytes and albumin: Structures correlate to
function.";
Eur. J. Microbiol. Immunol. 3:152-162(2013).
[8]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 229-683 IN COMPLEX WITH
CALCIUM, AND ACTIVE SITE.
STRAIN=ATCC BAA-308 / W83 {ECO:0000303|PubMed:25266723};
PubMed=25266723; DOI=10.1074/jbc.M114.602052;
de Diego I., Veillard F., Sztukowska M.N., Guevara T., Potempa B.,
Pomowski A., Huntington J.A., Potempa J., Gomis-Ruth F.X.;
"Structure and mechanism of cysteine peptidase gingipain K (Kgp), a
major virulence factor of Porphyromonas gingivalis in periodontitis.";
J. Biol. Chem. 289:32291-32302(2014).
[9]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 229-680.
STRAIN=ATCC 53978 / W50 {ECO:0000303|PubMed:25327141};
PubMed=25327141; DOI=10.1002/pro.2589;
Gorman M.A., Seers C.A., Michell B.J., Feil S.C., Huq N.L.,
Cross K.J., Reynolds E.C., Parker M.W.;
"Structure of the lysine specific protease Kgp from Porphyromonas
gingivalis, a target for improved oral health.";
Protein Sci. 24:162-166(2015).
-!- FUNCTION: Cysteine proteinase with a strong preference for
substrates with Lys in the P1 position. Hydrolyzes bovine
hemoglobin, bovine serum albumin, casein, human placental type I
collagen and human IgA and IgG (PubMed:9245829). Disrupts the
functions of polymorphonuclear leukocytes. May act as a virulence
factor in the development of peridontal disease. Involved in the
coaggregation of P.gingivalis with other oral bacteria (By
similarity). Has hemolytic activity; this is mediated by the
adhesin domains and does not require the catalytic domain
(PubMed:21812842, PubMed:24265933). {ECO:0000250|UniProtKB:B2RLK2,
ECO:0000269|PubMed:24265933, ECO:0000269|PubMed:9245829}.
-!- CATALYTIC ACTIVITY: Endopeptidase with strict specificity for
lysyl bonds. {ECO:0000269|PubMed:9245829}.
-!- SUBCELLULAR LOCATION: Lys-gingipain catalytic subunit: Secreted,
extracellular space {ECO:0000269|PubMed:9245829}.
-!- SUBCELLULAR LOCATION: 39 kDa adhesin: Secreted, extracellular
space {ECO:0000269|PubMed:9245829}.
-!- SUBCELLULAR LOCATION: 15 kDa adhesin: Secreted, extracellular
space {ECO:0000269|PubMed:9245829}.
-!- SUBCELLULAR LOCATION: 44 kDa adhesin: Secreted, extracellular
space {ECO:0000269|PubMed:9245829}.
-!- DOMAIN: The isolated adhesin domains have hemolytic activity (in
vitro). {ECO:0000269|PubMed:21812842,
ECO:0000269|PubMed:24265933}.
-!- PTM: Proteolytically cleaved into a catalytic subunit and three
adhesins. Arg-gingipain is involved in this post-translational
processing. {ECO:0000269|PubMed:9245829}.
-!- POLYMORPHISM: Several forms of kgp with differences at the C-
terminus exist in different P.gingivalis strains.
{ECO:0000269|PubMed:15297553}.
-!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000255}.
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EMBL; U42210; AAB06565.1; -; Genomic_DNA.
EMBL; AF017059; AAC26523.1; -; Genomic_DNA.
EMBL; U75366; AAB60809.1; -; Genomic_DNA.
PIR; T30836; T30836.
PDB; 3M1H; X-ray; 1.56 A; A/B/C/D=1427-1602.
PDB; 4ITC; X-ray; 1.55 A; A=982-1154.
PDB; 4RBM; X-ray; 1.75 A; A=229-683.
PDB; 4TKX; X-ray; 1.60 A; L=229-680.
PDB; 5MUN; X-ray; 1.80 A; A/B=20-228.
PDBsum; 3M1H; -.
PDBsum; 4ITC; -.
PDBsum; 4RBM; -.
PDBsum; 4TKX; -.
PDBsum; 5MUN; -.
ProteinModelPortal; Q51817; -.
SMR; Q51817; -.
PRIDE; Q51817; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0044179; P:hemolysis in other organism; IMP:UniProtKB.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
CDD; cd10913; Peptidase_C25_N_gingipain; 1.
Gene3D; 2.60.40.10; -; 4.
Gene3D; 2.60.40.3800; -; 1.
Gene3D; 3.40.50.10390; -; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR011628; Cleaved_adhesin.
InterPro; IPR001769; Gingipain.
InterPro; IPR039392; Gingipain_N.
InterPro; IPR029031; Gingipain_N_sf.
InterPro; IPR038490; Gingipain_propep_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR018832; Pept_C25_gingipain_C.
InterPro; IPR005536; Peptidase_C25_Ig-like_domain.
InterPro; IPR012600; Propeptide_C25.
Pfam; PF07675; Cleaved_Adhesin; 3.
Pfam; PF10365; DUF2436; 1.
Pfam; PF01364; Peptidase_C25; 1.
Pfam; PF03785; Peptidase_C25_C; 1.
Pfam; PF08126; Propeptide_C25; 1.
SUPFAM; SSF52129; SSF52129; 1.
1: Evidence at protein level;
3D-structure; Calcium; Direct protein sequencing; Hydrolase;
Metal-binding; Protease; Secreted; Signal; Thiol protease; Virulence;
Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 228 {ECO:0000269|PubMed:9245829}.
/FTId=PRO_0000395381.
CHAIN 229 1732 Lys-gingipain W83.
{ECO:0000305|PubMed:9245829}.
/FTId=PRO_0000395382.
CHAIN 229 680 Lys-gingipain catalytic subunit.
{ECO:0000305|PubMed:25327141,
ECO:0000305|PubMed:9245829}.
/FTId=PRO_0000395383.
CHAIN 738 ? 39 kDa adhesin.
{ECO:0000305|PubMed:9245829}.
/FTId=PRO_0000395384.
CHAIN 1157 ? 15 kDa adhesin.
{ECO:0000305|PubMed:9245829}.
/FTId=PRO_0000395385.
CHAIN 1292 ? 44 kDa adhesin.
{ECO:0000305|PubMed:21812842,
ECO:0000305|PubMed:9245829}.
/FTId=PRO_0000395386.
ACT_SITE 444 444 Proton donor.
{ECO:0000305|PubMed:25266723}.
ACT_SITE 477 477 Nucleophile.
{ECO:0000269|PubMed:25266723}.
METAL 313 313 Calcium 1. {ECO:0000244|PDB:4RBM,
ECO:0000269|PubMed:25266723}.
METAL 337 337 Calcium 2. {ECO:0000244|PDB:4RBM,
ECO:0000269|PubMed:25266723}.
METAL 339 339 Calcium 2. {ECO:0000244|PDB:4RBM,
ECO:0000269|PubMed:25266723}.
METAL 341 341 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:4RBM,
ECO:0000269|PubMed:25266723}.
METAL 343 343 Calcium 2. {ECO:0000244|PDB:4RBM,
ECO:0000269|PubMed:25266723}.
METAL 482 482 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:4RBM,
ECO:0000269|PubMed:25266723}.
METAL 491 491 Calcium 1. {ECO:0000244|PDB:4RBM,
ECO:0000269|PubMed:25266723}.
METAL 988 988 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 990 990 Calcium 3. {ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1001 1001 Calcium 4. {ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1003 1003 Calcium 4. {ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1005 1005 Calcium 4. {ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1007 1007 Calcium 4; via carbonyl oxygen.
{ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1022 1022 Calcium 3. {ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1024 1024 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1043 1043 Calcium 4. {ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1146 1146 Calcium 3. {ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1147 1147 Calcium 3. {ECO:0000244|PDB:4ITC,
ECO:0000269|PubMed:24265933}.
METAL 1433 1433 Calcium 5; via carbonyl oxygen.
{ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1435 1435 Calcium 5. {ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1446 1446 Calcium 6. {ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1448 1448 Calcium 6. {ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1450 1450 Calcium 6. {ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1452 1452 Calcium 6; via carbonyl oxygen.
{ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1470 1470 Calcium 5. {ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1472 1472 Calcium 5; via carbonyl oxygen.
{ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1490 1490 Calcium 6. {ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
METAL 1595 1595 Calcium 5. {ECO:0000244|PDB:3M1H,
ECO:0000269|PubMed:21812842}.
SITE 228 229 Cleavage; site 1.
{ECO:0000269|PubMed:9245829}.
SITE 737 738 Cleavage; site 2.
{ECO:0000269|PubMed:9245829}.
SITE 1156 1157 Cleavage; site 3.
{ECO:0000269|PubMed:9245829}.
SITE 1291 1292 Cleavage; site 4.
{ECO:0000269|PubMed:9245829}.
CONFLICT 796 796 V -> I (in Ref. 3; AAB60809).
{ECO:0000305}.
CONFLICT 1351 1351 K -> N (in Ref. 2; AAC26523).
{ECO:0000305}.
CONFLICT 1364 1364 D -> Y (in Ref. 2; AAC26523).
{ECO:0000305}.
CONFLICT 1390 1390 D -> N (in Ref. 3; AAB60809).
{ECO:0000305}.
CONFLICT 1448 1448 D -> H (in Ref. 2; AAC26523).
{ECO:0000305}.
CONFLICT 1479 1479 H -> Y (in Ref. 3; AAB60809).
{ECO:0000305}.
STRAND 22 25 {ECO:0000244|PDB:5MUN}.
STRAND 27 30 {ECO:0000244|PDB:5MUN}.
STRAND 32 39 {ECO:0000244|PDB:5MUN}.
STRAND 42 48 {ECO:0000244|PDB:5MUN}.
STRAND 50 59 {ECO:0000244|PDB:5MUN}.
STRAND 62 68 {ECO:0000244|PDB:5MUN}.
STRAND 73 75 {ECO:0000244|PDB:5MUN}.
STRAND 83 92 {ECO:0000244|PDB:5MUN}.
STRAND 97 111 {ECO:0000244|PDB:5MUN}.
TURN 113 115 {ECO:0000244|PDB:5MUN}.
HELIX 133 135 {ECO:0000244|PDB:5MUN}.
HELIX 144 146 {ECO:0000244|PDB:5MUN}.
STRAND 155 164 {ECO:0000244|PDB:5MUN}.
STRAND 167 174 {ECO:0000244|PDB:5MUN}.
STRAND 177 180 {ECO:0000244|PDB:5MUN}.
TURN 181 184 {ECO:0000244|PDB:5MUN}.
STRAND 185 199 {ECO:0000244|PDB:5MUN}.
HELIX 230 233 {ECO:0000244|PDB:4TKX}.
STRAND 240 248 {ECO:0000244|PDB:4TKX}.
HELIX 250 252 {ECO:0000244|PDB:4TKX}.
HELIX 253 265 {ECO:0000244|PDB:4TKX}.
STRAND 268 274 {ECO:0000244|PDB:4TKX}.
TURN 278 280 {ECO:0000244|PDB:4TKX}.
HELIX 284 300 {ECO:0000244|PDB:4TKX}.
STRAND 306 312 {ECO:0000244|PDB:4TKX}.
TURN 314 316 {ECO:0000244|PDB:4TKX}.
TURN 323 325 {ECO:0000244|PDB:4TKX}.
STRAND 327 330 {ECO:0000244|PDB:4TKX}.
HELIX 331 334 {ECO:0000244|PDB:4TKX}.
STRAND 337 341 {ECO:0000244|PDB:4RBM}.
STRAND 343 349 {ECO:0000244|PDB:4TKX}.
HELIX 354 369 {ECO:0000244|PDB:4TKX}.
HELIX 375 379 {ECO:0000244|PDB:4TKX}.
STRAND 380 385 {ECO:0000244|PDB:4TKX}.
HELIX 391 394 {ECO:0000244|PDB:4TKX}.
HELIX 396 406 {ECO:0000244|PDB:4TKX}.
HELIX 410 412 {ECO:0000244|PDB:4TKX}.
STRAND 415 420 {ECO:0000244|PDB:4TKX}.
TURN 426 429 {ECO:0000244|PDB:4TKX}.
HELIX 430 434 {ECO:0000244|PDB:4TKX}.
STRAND 437 443 {ECO:0000244|PDB:4TKX}.
TURN 451 454 {ECO:0000244|PDB:4TKX}.
HELIX 457 461 {ECO:0000244|PDB:4TKX}.
STRAND 470 478 {ECO:0000244|PDB:4TKX}.
STRAND 484 486 {ECO:0000244|PDB:4TKX}.
HELIX 489 495 {ECO:0000244|PDB:4TKX}.
STRAND 499 509 {ECO:0000244|PDB:4TKX}.
HELIX 513 521 {ECO:0000244|PDB:4TKX}.
TURN 533 535 {ECO:0000244|PDB:4TKX}.
HELIX 540 545 {ECO:0000244|PDB:4TKX}.
STRAND 547 549 {ECO:0000244|PDB:4TKX}.
HELIX 553 569 {ECO:0000244|PDB:4TKX}.
HELIX 578 584 {ECO:0000244|PDB:4TKX}.
STRAND 585 589 {ECO:0000244|PDB:4TKX}.
STRAND 616 622 {ECO:0000244|PDB:4TKX}.
STRAND 627 632 {ECO:0000244|PDB:4TKX}.
STRAND 635 642 {ECO:0000244|PDB:4TKX}.
STRAND 646 654 {ECO:0000244|PDB:4TKX}.
STRAND 660 667 {ECO:0000244|PDB:4TKX}.
STRAND 674 680 {ECO:0000244|PDB:4TKX}.
STRAND 984 987 {ECO:0000244|PDB:4ITC}.
STRAND 997 1001 {ECO:0000244|PDB:4ITC}.
STRAND 1010 1013 {ECO:0000244|PDB:4ITC}.
TURN 1014 1016 {ECO:0000244|PDB:4ITC}.
STRAND 1022 1032 {ECO:0000244|PDB:4ITC}.
TURN 1033 1036 {ECO:0000244|PDB:4ITC}.
STRAND 1043 1046 {ECO:0000244|PDB:4ITC}.
STRAND 1056 1066 {ECO:0000244|PDB:4ITC}.
STRAND 1073 1081 {ECO:0000244|PDB:4ITC}.
HELIX 1085 1087 {ECO:0000244|PDB:4ITC}.
STRAND 1090 1096 {ECO:0000244|PDB:4ITC}.
STRAND 1117 1123 {ECO:0000244|PDB:4ITC}.
STRAND 1129 1134 {ECO:0000244|PDB:4ITC}.
STRAND 1142 1152 {ECO:0000244|PDB:4ITC}.
STRAND 1428 1432 {ECO:0000244|PDB:3M1H}.
STRAND 1442 1448 {ECO:0000244|PDB:3M1H}.
STRAND 1454 1457 {ECO:0000244|PDB:3M1H}.
TURN 1459 1462 {ECO:0000244|PDB:3M1H}.
STRAND 1474 1480 {ECO:0000244|PDB:3M1H}.
TURN 1481 1483 {ECO:0000244|PDB:3M1H}.
STRAND 1489 1493 {ECO:0000244|PDB:3M1H}.
STRAND 1503 1513 {ECO:0000244|PDB:3M1H}.
STRAND 1520 1528 {ECO:0000244|PDB:3M1H}.
HELIX 1532 1534 {ECO:0000244|PDB:3M1H}.
STRAND 1539 1543 {ECO:0000244|PDB:3M1H}.
STRAND 1566 1572 {ECO:0000244|PDB:3M1H}.
STRAND 1578 1585 {ECO:0000244|PDB:3M1H}.
STRAND 1591 1601 {ECO:0000244|PDB:3M1H}.
SEQUENCE 1732 AA; 187875 MW; 654271DBEF7BCAE4 CRC64;
MRKLLLLIAA SLLGVGLYAQ SAKIKLDAPT TRTTCTNNSF KQFDASFSFN EVELTKVETK
GGTFASVSIP GAFPTGEVGS PEVPAVRKLI AVPVGATPVV RVKSFTEQVY SLNQYGSEKL
MPHQPSMSKS DDPEKVPFVY NAAAYARKGF VGQELTQVEM LGTMRGVRIA ALTINPVQYD
VVANQLKVRN NIEIEVSFQG ADEVATQRLY DASFSPYFET AYKQLFNRDV YTDHGDLYNT
PVRMLVVAGA KFKEALKPWL TWKAQKGFYL DVHYTDEAEV GTTNASIKAF IHKKYNDGLA
ASAAPVFLAL VGDTDVISGE KGKKTKKVTD LYYSAVDGDY FPEMYTFRMS ASSPEELTNI
IDKVLMYEKA TMPDKSYLEK VLLIAGADYS WNSQVGQPTI KYGMQYYYNQ EHGYTDVYNY
LKAPYTGCYS HLNTGVSFAN YTAHGSETAW ADPLLTTSQL KALTNKDKYF LAIGNCCITA
QFDYVQPCFG EVITRVKEKG AYAYIGSSPN SYWGEDYYWS VGANAVFGVQ PTFEGTSMGS
YDATFLEDSY NTVNSIMWAG NLAATHAGNI GNITHIGAHY YWEAYHVLGD GSVMPYRAMP
KTNTYTLPAS LPQNQASYSI QASAGSYVAI SKDGVLYGTG VANASGVATV SMTKQITENG
NYDVVITRSN YLPVIKQIQV GEPSPYQPVS NLTATTQGQK VTLKWEAPSA KKAEGSREVK
RIGDGLFVTI EPANDVRANE AKVVLAADNV WGDNTGYQFL LDADHNTFGS VIPATGPLFT
GTASSNLYSA NFEYLVPANA DPVVTTQNII VTGQGEVVIP GGVYDYCITN PEPASGKMWI
AGDGGNQPAR YDDFTFEAGK KYTFTMRRAG MGDGTDMEVE DDSPASYTYT VYRDGTKIKE
GLTATTFEED GVAAGNHEYC VEVKYTAGVS PKVCKDVTVE GSNEFAPVQN LTGSSVGQKV
TLKWDAPNGT PNPNPNPNPN PGTTLSESFE NGIPASWKTI DADGDGHGWK PGNAPGIAGY
NSNGCVYSES FGLGGIGVLT PDNYLITPAL DLPNGGKLTF WVCAQDANYA SEHYAVYASS
TGNDASNFTN ALLEETITAK GVRSPKAIRG RIQGTWRQKT VDLPAGTKYV AFRHFQSTDM
FYIDLDEVEI KANGKRADFT ETFESSTHGE APAEWTTIDA DGDGQGWLCL SSGQLDWLTA
HGGSNVVSSF SWNGMALNPD NYLISKDVTG ATKVKYYYAV NDGFPGDHYA VMISKTGTNA
GDFTVVFEET PNGINKGGAR FGLSTEANGA KPQSVWIERT VDLPAGTKYV AFRHYNCSDL
NYILLDDIQF TMGGSPTPTD YTYTVYRDGT KIKEGLTETT FEEDGVATGN HEYCVEVKYT
AGVSPKKCVD VTVNSTQFNP VQNLTAEQAP NSMDAILKWN APASKRAEVL NEDFENGIPA
SWKTIDADGD GNNWTTTPPP GGSSFAGHNS AICVSSASHI NFEGPQNPDN YLVTPELSLP
GGGTLTFWVC AQDANYASEH YAVYASSTGN DASNFANALL EEVLTAKTVV TAPEAIRGTR
AQGTWYQKTV QLPAGTKYVA FRHFGCTDFF WINLDDVVIT SGNAPSYTYT IYRNNTQIAS
GVTETTYRDP DLATGFYTYG VKVVYPNGES AIETATLNIT SLADVTAQKP YTLTVVGKTI
TVTCQGEAMI YDMNGRRLAA GRNTVVYTAQ GGHYAVMVVV DGKSYVEKLA VK


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