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 13-SEP-2023, entry version 100. 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}, prtP GN {ECO:0000303|PubMed:9632563, ECO:0000312|EMBL:AAB06565.1}; OS Porphyromonas gingivalis. OC Bacteria; Bacteroidota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; 2.60.120.200; -; 3. DR Gene3D; 2.60.40.3800; -; 1. DR Gene3D; 3.40.50.1460; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. 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 NCBIfam; NF038128; choice_anch_J; 3. 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; Caspase-like; 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 //