KGP83_PORGN
ID KGP83_PORGN Reviewed; 1732 AA.
AC Q51817; O07442; O52050;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Lys-gingipain W83 {ECO:0000250|UniProtKB:B2RLK2, ECO:0000303|PubMed:15297553};
DE EC=3.4.22.47 {ECO:0000269|PubMed:9245829};
DE AltName: Full=Lysine specific cysteine protease {ECO:0000303|PubMed:9632563, ECO:0000312|EMBL:AAC26523.1};
DE AltName: Full=Lysine-specific cysteine proteinase {ECO:0000303|PubMed:10219167, ECO:0000312|EMBL:AAB60809.1};
DE AltName: Full=Porphypain {ECO:0000303|PubMed:8631659, ECO:0000312|EMBL:AAB06565.1};
DE AltName: Full=PrtK48 {ECO:0000303|PubMed:10219167};
DE Contains:
DE RecName: Full=Lys-gingipain catalytic subunit {ECO:0000250|UniProtKB:B2RLK2, ECO:0000303|PubMed:9245829};
DE Contains:
DE RecName: Full=39 kDa adhesin {ECO:0000303|PubMed:9245829};
DE AltName: Full=PrtK39 {ECO:0000303|PubMed:10219167};
DE Contains:
DE RecName: Full=15 kDa adhesin {ECO:0000303|PubMed:9245829};
DE AltName: Full=PrtK15 {ECO:0000303|PubMed:10219167};
DE Contains:
DE RecName: Full=44 kDa adhesin {ECO:0000303|PubMed:9245829};
DE AltName: Full=PrtK44 {ECO:0000303|PubMed:10219167};
DE Flags: Precursor;
GN Name=kgp {ECO:0000250|UniProtKB:B2RLK2};
GN Synonyms=prtK {ECO:0000312|EMBL:AAB60809.1},
GN prtP {ECO:0000303|PubMed:9632563, ECO:0000312|EMBL:AAB06565.1};
OS Porphyromonas gingivalis.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=837;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB06565.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W12 {ECO:0000312|EMBL:AAB06565.1};
RX PubMed=8631659; DOI=10.1128/jb.178.10.2734-2741.1996;
RA Barkocy-Gallagher G.A., Han N., Patti J.M., Whitlock J., Progulske-Fox A.,
RA Lantz M.S.;
RT "Analysis of the prtP gene encoding porphypain, a cysteine proteinase of
RT Porphyromonas gingivalis.";
RL J. Bacteriol. 178:2734-2741(1996).
RN [2] {ECO:0000312|EMBL:AAC26523.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000312|EMBL:AAC26523.1};
RX PubMed=9632563; DOI=10.1128/iai.66.7.3035-3042.1998;
RA Lewis J.P., Macrina F.L.;
RT "IS195, an insertion sequence-like element associated with protease genes
RT in Porphyromonas gingivalis.";
RL Infect. Immun. 66:3035-3042(1998).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAB60809.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 53978 / W50 {ECO:0000312|EMBL:AAB60809.1};
RX PubMed=10219167; DOI=10.1034/j.1399-302x.1999.140203.x;
RA Slakeski N., Cleal S.M., Bhogal P.S., Reynolds E.C.;
RT "Characterization of a Porphyromonas gingivalis gene prtK that encodes a
RT lysine-specific cysteine proteinase and three sequence-related adhesins.";
RL Oral Microbiol. Immunol. 14:92-97(1999).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 229-245; 738-763; 1157-1180 AND 1292-1313, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 53978 / W50 {ECO:0000269|PubMed:9245829};
RX PubMed=9245829; DOI=10.1099/00221287-143-7-2485;
RA Bhogal P.S., Slakeski N., Reynolds E.C.;
RT "A cell-associated protein complex of Porphyromonas gingivalis W50 composed
RT of Arg- and Lys-specific cysteine proteinases and adhesins.";
RL Microbiology 143:2485-2495(1997).
RN [5] {ECO:0000305}
RP POLYMORPHISM.
RX PubMed=15297553; DOI=10.1128/jcm.42.8.3873-3876.2004;
RA Nadkarni M.A., Nguyen K.A., Chapple C.C., DeCarlo A.A., Jacques N.A.,
RA Hunter N.;
RT "Distribution of Porphyromonas gingivalis biotypes defined by alleles of
RT the kgp (Lys-gingipain) gene.";
RL J. Clin. Microbiol. 42:3873-3876(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 1427-1602 IN COMPLEX WITH
RP CALCIUM, DOMAIN, AND FUNCTION.
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000303|PubMed:21812842};
RX PubMed=21812842; DOI=10.1111/j.1365-2958.2011.07768.x;
RA Li N., Yun P., Jeffries C.M., Langley D., Gamsjaeger R., Church W.B.,
RA Hunter N., Collyer C.A.;
RT "The modular structure of haemagglutinin/adhesin regions in gingipains of
RT Porphyromonas gingivalis.";
RL Mol. Microbiol. 81:1358-1373(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 982-1154 IN COMPLEX WITH CALCIUM,
RP AND FUNCTION.
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000303|PubMed:24265933};
RX PubMed=24265933; DOI=10.1556/eujmi.3.2013.3.2;
RA Ganuelas L.A., Li N., Yun P., Hunter N., Collyer C.A.;
RT "The lysine gingipain adhesin domains from Porphyromonas gingivalis
RT interact with erythrocytes and albumin: Structures correlate to function.";
RL Eur. J. Microbiol. Immunol. 3:152-162(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 229-683 IN COMPLEX WITH CALCIUM,
RP AND ACTIVE SITE.
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000303|PubMed:25266723};
RX PubMed=25266723; DOI=10.1074/jbc.m114.602052;
RA de Diego I., Veillard F., Sztukowska M.N., Guevara T., Potempa B.,
RA Pomowski A., Huntington J.A., Potempa J., Gomis-Ruth F.X.;
RT "Structure and mechanism of cysteine peptidase gingipain K (Kgp), a major
RT virulence factor of Porphyromonas gingivalis in periodontitis.";
RL J. Biol. Chem. 289:32291-32302(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 229-680.
RC STRAIN=ATCC 53978 / W50 {ECO:0000303|PubMed:25327141};
RX PubMed=25327141; DOI=10.1002/pro.2589;
RA Gorman M.A., Seers C.A., Michell B.J., Feil S.C., Huq N.L., Cross K.J.,
RA Reynolds E.C., Parker M.W.;
RT "Structure of the lysine specific protease Kgp from Porphyromonas
RT gingivalis, a target for improved oral health.";
RL Protein Sci. 24:162-166(2015).
CC -!- FUNCTION: Cysteine proteinase with a strong preference for substrates
CC with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum
CC albumin, casein, human placental type I collagen and human IgA and IgG
CC (PubMed:9245829). Disrupts the functions of polymorphonuclear
CC leukocytes. May act as a virulence factor in the development of
CC peridontal disease. Involved in the coaggregation of P.gingivalis with
CC other oral bacteria (By similarity). Has hemolytic activity; this is
CC mediated by the adhesin domains and does not require the catalytic
CC domain (PubMed:21812842, PubMed:24265933).
CC {ECO:0000250|UniProtKB:B2RLK2, ECO:0000269|PubMed:24265933,
CC ECO:0000269|PubMed:9245829}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with strict specificity for lysyl bonds.;
CC EC=3.4.22.47; Evidence={ECO:0000269|PubMed:9245829};
CC -!- SUBCELLULAR LOCATION: [Lys-gingipain catalytic subunit]: Secreted
CC {ECO:0000269|PubMed:9245829}.
CC -!- SUBCELLULAR LOCATION: [39 kDa adhesin]: Secreted
CC {ECO:0000269|PubMed:9245829}.
CC -!- SUBCELLULAR LOCATION: [15 kDa adhesin]: Secreted
CC {ECO:0000269|PubMed:9245829}.
CC -!- SUBCELLULAR LOCATION: [44 kDa adhesin]: Secreted
CC {ECO:0000269|PubMed:9245829}.
CC -!- DOMAIN: The isolated adhesin domains have hemolytic activity (in
CC vitro). {ECO:0000269|PubMed:21812842, ECO:0000269|PubMed:24265933}.
CC -!- PTM: Proteolytically cleaved into a catalytic subunit and three
CC adhesins. Arg-gingipain is involved in this post-translational
CC processing. {ECO:0000269|PubMed:9245829}.
CC -!- POLYMORPHISM: Several forms of kgp with differences at the C-terminus
CC exist in different P.gingivalis strains. {ECO:0000269|PubMed:15297553}.
CC -!- SIMILARITY: Belongs to the peptidase C25 family. {ECO:0000255}.
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DR EMBL; U42210; AAB06565.1; -; Genomic_DNA.
DR EMBL; AF017059; AAC26523.1; -; Genomic_DNA.
DR EMBL; U75366; AAB60809.1; -; Genomic_DNA.
DR PIR; T30836; T30836.
DR PDB; 3M1H; X-ray; 1.56 A; A/B/C/D=1427-1602.
DR PDB; 4ITC; X-ray; 1.55 A; A=982-1154.
DR PDB; 4RBM; X-ray; 1.75 A; A=229-683.
DR PDB; 4TKX; X-ray; 1.60 A; L=229-680.
DR PDB; 5MUN; X-ray; 1.80 A; A/B=20-228.
DR PDB; 6I9A; X-ray; 1.20 A; A/B=229-683.
DR PDBsum; 3M1H; -.
DR PDBsum; 4ITC; -.
DR PDBsum; 4RBM; -.
DR PDBsum; 4TKX; -.
DR PDBsum; 5MUN; -.
DR PDBsum; 6I9A; -.
DR AlphaFoldDB; Q51817; -.
DR SASBDB; Q51817; -.
DR SMR; Q51817; -.
DR BindingDB; Q51817; -.
DR MEROPS; C25.002; -.
DR PRIDE; Q51817; -.
DR BRENDA; 3.4.22.47; 756.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd10913; Peptidase_C25_N_gingipain; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 2.60.40.3800; -; 1.
DR Gene3D; 3.40.50.10390; -; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011628; Cleaved_adhesin.
DR InterPro; IPR001769; Gingipain.
DR InterPro; IPR039392; Gingipain_N.
DR InterPro; IPR029031; Gingipain_N_sf.
DR InterPro; IPR038490; Gingipain_propep_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR018832; Pept_C25_gingipain_C.
DR InterPro; IPR005536; Peptidase_C25_Ig-like_domain.
DR InterPro; IPR012600; Propeptide_C25.
DR Pfam; PF07675; Cleaved_Adhesin; 3.
DR Pfam; PF10365; DUF2436; 1.
DR Pfam; PF01364; Peptidase_C25; 1.
DR Pfam; PF03785; Peptidase_C25_C; 1.
DR Pfam; PF08126; Propeptide_C25; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Protease; Secreted; Signal; Thiol protease; Virulence; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..228
FT /evidence="ECO:0000269|PubMed:9245829"
FT /id="PRO_0000395381"
FT CHAIN 229..1732
FT /note="Lys-gingipain W83"
FT /evidence="ECO:0000305|PubMed:9245829"
FT /id="PRO_0000395382"
FT CHAIN 229..680
FT /note="Lys-gingipain catalytic subunit"
FT /evidence="ECO:0000305|PubMed:25327141,
FT ECO:0000305|PubMed:9245829"
FT /id="PRO_0000395383"
FT CHAIN 738..?
FT /note="39 kDa adhesin"
FT /evidence="ECO:0000305|PubMed:9245829"
FT /id="PRO_0000395384"
FT CHAIN 1157..?
FT /note="15 kDa adhesin"
FT /evidence="ECO:0000305|PubMed:9245829"
FT /id="PRO_0000395385"
FT CHAIN 1292..?
FT /note="44 kDa adhesin"
FT /evidence="ECO:0000305|PubMed:21812842,
FT ECO:0000305|PubMed:9245829"
FT /id="PRO_0000395386"
FT REGION 965..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 444
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:25266723"
FT ACT_SITE 477
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:25266723"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25266723,
FT ECO:0007744|PDB:4RBM"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25266723,
FT ECO:0007744|PDB:4RBM"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25266723,
FT ECO:0007744|PDB:4RBM"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25266723,
FT ECO:0007744|PDB:4RBM"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25266723,
FT ECO:0007744|PDB:4RBM"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25266723,
FT ECO:0007744|PDB:4RBM"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25266723,
FT ECO:0007744|PDB:4RBM"
FT BINDING 988
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 990
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1001
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1003
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1005
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1007
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1022
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1024
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1043
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24265933,
FT ECO:0007744|PDB:4ITC"
FT BINDING 1433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT BINDING 1595
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:21812842,
FT ECO:0007744|PDB:3M1H"
FT SITE 228..229
FT /note="Cleavage; site 1"
FT /evidence="ECO:0000269|PubMed:9245829"
FT SITE 737..738
FT /note="Cleavage; site 2"
FT /evidence="ECO:0000269|PubMed:9245829"
FT SITE 1156..1157
FT /note="Cleavage; site 3"
FT /evidence="ECO:0000269|PubMed:9245829"
FT SITE 1291..1292
FT /note="Cleavage; site 4"
FT /evidence="ECO:0000269|PubMed:9245829"
FT CONFLICT 796
FT /note="V -> I (in Ref. 3; AAB60809)"
FT /evidence="ECO:0000305"
FT CONFLICT 1351
FT /note="K -> N (in Ref. 2; AAC26523)"
FT /evidence="ECO:0000305"
FT CONFLICT 1364
FT /note="D -> Y (in Ref. 2; AAC26523)"
FT /evidence="ECO:0000305"
FT CONFLICT 1390
FT /note="D -> N (in Ref. 3; AAB60809)"
FT /evidence="ECO:0000305"
FT CONFLICT 1448
FT /note="D -> H (in Ref. 2; AAC26523)"
FT /evidence="ECO:0000305"
FT CONFLICT 1479
FT /note="H -> Y (in Ref. 3; AAB60809)"
FT /evidence="ECO:0000305"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 97..111
FT /evidence="ECO:0007829|PDB:5MUN"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5MUN"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5MUN"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:5MUN"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:5MUN"
FT STRAND 185..199
FT /evidence="ECO:0007829|PDB:5MUN"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:6I9A"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 284..300
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:6I9A"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6I9A"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 354..369
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 396..406
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:6I9A"
FT TURN 426..429
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:6I9A"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 489..495
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 499..509
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 513..521
FT /evidence="ECO:0007829|PDB:6I9A"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:4TKX"
FT HELIX 540..545
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 553..570
FT /evidence="ECO:0007829|PDB:6I9A"
FT HELIX 578..584
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 616..623
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 627..632
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 635..642
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 646..654
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 660..667
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 674..680
FT /evidence="ECO:0007829|PDB:6I9A"
FT STRAND 984..987
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 997..1001
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1010..1013
FT /evidence="ECO:0007829|PDB:4ITC"
FT TURN 1014..1016
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1022..1032
FT /evidence="ECO:0007829|PDB:4ITC"
FT TURN 1033..1036
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1043..1046
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1056..1066
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1073..1081
FT /evidence="ECO:0007829|PDB:4ITC"
FT HELIX 1085..1087
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1090..1096
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1117..1123
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1129..1134
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1142..1152
FT /evidence="ECO:0007829|PDB:4ITC"
FT STRAND 1428..1432
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1442..1448
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1454..1457
FT /evidence="ECO:0007829|PDB:3M1H"
FT TURN 1459..1462
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1474..1480
FT /evidence="ECO:0007829|PDB:3M1H"
FT TURN 1481..1483
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1489..1493
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1503..1513
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1520..1528
FT /evidence="ECO:0007829|PDB:3M1H"
FT HELIX 1532..1534
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1539..1543
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1566..1572
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1578..1585
FT /evidence="ECO:0007829|PDB:3M1H"
FT STRAND 1591..1601
FT /evidence="ECO:0007829|PDB:3M1H"
SQ 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
