COLY_YERPE
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 03-AUG-2022, entry version 157.
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}.
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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 AlphaFoldDB; P17811; -.
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 OMA; YNYDNGA; -.
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:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0007599; P:hemostasis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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
