ID COLY_YERPE Reviewed; 312 AA. AC P17811; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 02-JUN-2021, entry version 153. DE RecName: Full=Coagulase/fibrinolysin; DE EC=3.4.23.48; DE AltName: Full=Plasminogen activator; DE Flags: Precursor; GN Name=pla; OrderedLocusNames=YPPCP1.07, YP_pPCP08; OS Yersinia pestis. OG Plasmid pPCP1, and Plasmid pKYP1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=632; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=EV76-6; PLASMID=pKYP1; RX PubMed=2526282; DOI=10.1111/j.1365-2958.1989.tb00225.x; RA McDonough K.A., Falkow S.; RT "A Yersinia pestis-specific DNA fragment encodes temperature-dependent RT coagulase and fibrinolysin-associated phenotypes."; RL Mol. Microbiol. 3:767-775(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC PLASMID=pPCP1; RX PubMed=2651310; DOI=10.1128/iai.57.5.1517-1523.1989; RA Sodeinde O.A., Goguen J.D.; RT "Nucleotide sequence of the plasminogen activator gene of Yersinia pestis: RT relationship to ompT of Escherichia coli and gene E of Salmonella RT typhimurium."; RL Infect. Immun. 57:1517-1523(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=KIM5 / Biovar Mediaevalis; PLASMID=pPCP1; RX PubMed=9748454; DOI=10.1128/jb.180.19.5192-5202.1998; RA Hu P., Elliott J., McCready P., Skowronski E., Garnes J., Kobayashi A., RA Brubaker R.R., Garcia E.; RT "Structural organization of virulence-associated plasmids of Yersinia RT pestis."; RL J. Bacteriol. 180:5192-5202(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis; PLASMID=pPCP1; RX PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T., RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., RA Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91001 / Biovar Mediaevalis; PLASMID=pPCP1; RX PubMed=15368893; DOI=10.1093/dnares/11.3.179; RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., RA Wang J., Huang P., Yang R.; RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate RT avirulent to humans."; RL DNA Res. 11:179-197(2004). CC -!- FUNCTION: Seems to play an essential role in plague transmission by CC mediating flea blockage in a temperature-dependent fashion. CC Fibrinolytic activity prevails at 37 degrees Celsius whereas coagulase CC expression predominates at lower temperatures (<30 degrees Celsius). CC Activates plasminogen by cleaving it. CC -!- CATALYTIC ACTIVITY: CC Reaction=Converts human Glu-plasminogen to plasmin by cleaving the 560- CC Arg-|-Val-561 peptide bond that is also hydrolyzed by the mammalian CC u-plasminogen activator and t-plasminogen activator. Also cleaves CC arginyl bonds in other proteins.; EC=3.4.23.48; CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase A26 family. {ECO:0000305}. 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; X15136; CAA33235.1; -; Genomic_DNA. DR EMBL; M27820; AAA27667.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF053945; AAC62545.1; -; Genomic_DNA. DR EMBL; AL109969; CAB53170.1; -; Genomic_DNA. DR EMBL; AE017046; AAS58765.1; -; Genomic_DNA. DR PIR; A42928; A42928. DR PIR; S06979; A30916. DR RefSeq; NP_395233.1; NC_003132.1. DR RefSeq; NP_857784.1; NC_004837.1. DR RefSeq; WP_002218234.1; NZ_WUCM01000123.1. DR RefSeq; YP_006960975.1; NC_019235.1. DR PDB; 2X4M; X-ray; 2.55 A; A/B/C/D=21-312. DR PDB; 2X55; X-ray; 1.85 A; A=21-312. DR PDB; 2X56; X-ray; 2.30 A; A=21-312. DR PDB; 4DCB; X-ray; 2.03 A; A=25-312. DR PDBsum; 2X4M; -. DR PDBsum; 2X55; -. DR PDBsum; 2X56; -. DR PDBsum; 4DCB; -. DR SMR; P17811; -. DR IntAct; P17811; 1. DR MINT; P17811; -. DR ChEMBL; CHEMBL1075037; -. DR MEROPS; A26.003; -. DR DNASU; 1149148; -. DR EnsemblBacteria; AAS58765; AAS58765; YP_pPCP08. DR GeneID; 57977666; -. DR KEGG; ype:YPPCP1.07; -. DR KEGG; ypm:YP_pPCP08; -. DR PATRIC; fig|214092.21.peg.114; -. DR HOGENOM; CLU_063041_1_0_6; -. DR BRENDA; 3.4.23.48; 4559. DR BRENDA; 3.4.23.49; 4559. DR EvolutionaryTrace; P17811; -. DR PRO; PR:P17811; -. DR Proteomes; UP000000815; Plasmid pPCP1. DR Proteomes; UP000001019; Plasmid pPCP1. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW. DR InterPro; IPR020080; OM_adhesin/peptidase_omptin. DR InterPro; IPR020079; Peptidase_A26_CS. DR InterPro; IPR000036; Peptidase_A26_omptin. DR Pfam; PF01278; Omptin; 1. DR PIRSF; PIRSF001522; Peptidase_A26; 1. DR PRINTS; PR00482; OMPTIN. DR SUPFAM; SSF69917; SSF69917; 1. DR PROSITE; PS00834; OMPTIN_1; 1. DR PROSITE; PS00835; OMPTIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Aspartyl protease; Blood coagulation; Cell outer membrane; KW Fibrinolysis; Hemostasis; Hydrolase; Membrane; Plasmid; Protease; KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..312 FT /note="Coagulase/fibrinolysin" FT /id="PRO_0000025819" FT ACT_SITE 104 FT /evidence="ECO:0000250" FT ACT_SITE 106 FT /evidence="ECO:0000250" FT ACT_SITE 226 FT /evidence="ECO:0000250" FT ACT_SITE 228 FT /evidence="ECO:0000250" FT CONFLICT 279 FT /note="T -> I (in Ref. 5; AAS58765)" FT /evidence="ECO:0000305" FT HELIX 31..33 FT /evidence="ECO:0007829|PDB:4DCB" FT STRAND 34..52 FT /evidence="ECO:0007829|PDB:2X55" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 59..82 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 85..96 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 98..106 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 116..142 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 144..165 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:2X55" FT TURN 171..174 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 184..205 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 208..228 FT /evidence="ECO:0007829|PDB:2X55" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 233..256 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 259..270 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 275..280 FT /evidence="ECO:0007829|PDB:4DCB" FT TURN 282..284 FT /evidence="ECO:0007829|PDB:2X4M" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:2X55" FT STRAND 295..312 FT /evidence="ECO:0007829|PDB:2X55" SQ SEQUENCE 312 AA; 34611 MW; 52B7CB4F32E8FBE9 CRC64; MKKSSIVATI ITILSGSANA ASSQLIPNIS PDSFTVAAST GMLSGKSHEM LYDAETGRKI SQLDWKIKNV AILKGDISWD PYSFLTLNAR GWTSLASGSG NMDDYDWMNE NQSEWTDHSS HPATNVNHAN EYDLNVKGWL LQDENYKAGI TAGYQETRFS WTATGGSYSY NNGAYTGNFP KGVRVIGYNQ RFSMPYIGLA GQYRINDFEL NALFKFSDWV RAHDNDEHYM RDLTFREKTS GSRYYGTVIN AGYYVTPNAK VFAEFTYSKY DEGKGGTQTI DKNSGDSVSI GGDAAGISNK NYTVTAGLQY RF //