ID COLY_YERPE STANDARD; PRT; 312 AA. AC P17811; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Coagulase/fibrinolysin precursor (EC 3.4.23.-) (Plasminogen DE activator). GN PLA OR YPPCP1.07. OS Yersinia pestis. OG Plasmid pPCP1, and Plasmid pKYP1. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Yersinia. OX NCBI_TaxID=632; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=EV76-6; PLASMID=pKYP1; RX MEDLINE=89313306; PubMed=2526282; 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 SEQUENCE FROM N.A. RC PLASMID=pPCP1; RX MEDLINE=89212901; PubMed=2651310; RA Sodeinde O.A., Goguen J.D.; RT "Nucleotide sequence of the plasminogen activator gene of Yersinia RT pestis: relationship to ompT of Escherichia coli and gene E of RT Salmonella typhimurium."; RL Infect. Immun. 57:1517-1523(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CO-92 / Biovar Orientalis; PLASMID=pPCP1; RX MEDLINE=21470413; PubMed=11586360; 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., 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., RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., RA Leather S., Moule S., Oyston P.C.F., Quail M., Rutherford K., RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). CC -!- FUNCTION: SEEMS TO PLAY AN ESSENTIAL ROLE IN PLAGUE TRANSMISSION CC BY MEDIATING FLEA BLOCKAGE IN A TEMPERATURE-DEPENDENT FASHION. CC FIBRINOLYTIC ACTIVITY PREVAILS AT 37 DEGREES CELSIUS WHEREAS CC COAGULASE EXPRESSION PREDOMINATES AT LOWER TEMPERATURES (<30 CC DEGREES CELSIUS). ACTIVATES PLASMINOGEN BY CLEAVING IT. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Outer membrane CC (By similarity). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY A26. 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; -. DR EMBL; M27820; AAA27667.1; ALT_SEQ. DR EMBL; AL109969; CAB53170.1; -. DR PIR; A30916; A30916. DR PIR; A42928; A42928. DR PIR; S06979; S06979. DR HSSP; P09169; 1I78. DR MEROPS; A26.003; -. DR InterPro; IPR000036; Omptin. DR Pfam; PF01278; Omptin; 1. DR PRINTS; PR00482; OMPTIN. DR ProDom; PD011585; Omptin; 1. DR PROSITE; PS00834; OMPTIN_1; 1. DR PROSITE; PS00835; OMPTIN_2; 1. KW Hydrolase; Aspartyl protease; Outer membrane; Transmembrane; Signal; KW Plasmid; Complete proteome. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 312 COAGULASE/FIBRINOLYSIN. FT ACT_SITE 104 104 BY SIMILARITY. FT ACT_SITE 106 106 BY SIMILARITY. FT ACT_SITE 226 226 BY SIMILARITY. FT ACT_SITE 228 228 BY SIMILARITY. 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 //