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 01-OCT-1996 (Rel. 34, Last annotation update) DE COAGULASE/FIBRINOLYSIN PRECURSOR (EC 3.4.21.-) (PLASMINOGEN DE ACTIVATOR). GN PLA. OS Yersinia pestis. OG Plasmid pKYP1, and Plasmid pPCP1. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Yersinia. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=EV76-6; PLASMID=PKYP1; RX MEDLINE; 89313306. 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. 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). 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 -!- SUBUNIT: HOMOPENTAMER (POSSIBLE). CC -!- SUBCELLULAR LOCATION: OUTER MEMBRANE. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S18; ALSO KNOWN AS THE CC OMPTIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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 PIR; A30916; A30916. DR PIR; A42928; A42928. DR PIR; S06979; S06979. DR INTERPRO; IPR000036; -. DR PFAM; PF01278; Omptin; 1. DR PRINTS; PR00482; OMPTIN. DR PROSITE; PS00834; OMPTIN_1; 1. DR PROSITE; PS00835; OMPTIN_2; 1. KW Hydrolase; Serine protease; Outer membrane; Signal; Plasmid. FT SIGNAL 1 20 POTENTIAL. FT CHAIN 21 312 COAGULASE/FIBRINOLYSIN. 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 //