CAF1M_YERPE
ID CAF1M_YERPE Reviewed; 258 AA.
AC P26926; O68774; Q9RIB9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=Chaperone protein caf1M;
DE AltName: Full=Capsule protein fraction 1;
DE Flags: Precursor;
GN Name=caf1M; OrderedLocusNames=YPMT1.82, Y1098, YP_pMT084;
OS Yersinia pestis.
OG Plasmid pMT1 (pMT-1), and Plasmid pFra.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pFra;
RX PubMed=1677900; DOI=10.1016/0014-5793(91)80945-y;
RA Galyov E.E., Karlishev A.V., Chernovskaya T.V., Dolgikh D.A., Smirnov O.Y.,
RA Volkovoy K.I., Abramov V.M., Zav'Yalov V.P.;
RT "Expression of the envelope antigen F1 of Yersinia pestis is mediated by
RT the product of caf1M gene having homology with the chaperone protein PapD
RT of Escherichia coli.";
RL FEBS Lett. 286:79-82(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis; PLASMID=pMT1 (pMT-1);
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis; PLASMID=pMT1 (pMT-1);
RX PubMed=9826348; DOI=10.1128/iai.66.12.5731-5742.1998;
RA Lindler L.E., Plano G.V., Burland V., Mayhew G.F., Blattner F.R.;
RT "Complete DNA sequence and detailed analysis of the Yersinia pestis KIM5
RT plasmid encoding murine toxin and capsular antigen.";
RL Infect. Immun. 66:5731-5742(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis; PLASMID=pMT1 (pMT-1);
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=pMT1 (pMT-1);
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: Has a stimulatory role for the envelope antigen F1 secretion.
CC It seems to interact with the subunit polypeptide and to prevent it
CC from digestion by a protease.
CC -!- INTERACTION:
CC P26926; P26948: caf1; NbExp=6; IntAct=EBI-1036581, EBI-1036572;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC82756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS58716.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X61996; CAA43967.1; -; Genomic_DNA.
DR EMBL; AF074611; AAC82756.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF053947; AAC13220.1; -; Genomic_DNA.
DR EMBL; AL117211; CAB55264.1; -; Genomic_DNA.
DR EMBL; AE017045; AAS58716.1; ALT_INIT; Genomic_DNA.
DR PIR; S16965; S16965.
DR PIR; T14704; T14704.
DR PIR; T15013; T15013.
DR RefSeq; NP_395428.1; NC_003134.1.
DR RefSeq; NP_857694.1; NC_004835.1.
DR RefSeq; WP_002211762.1; NZ_WUCM01000058.1.
DR PDB; 1P5U; X-ray; 1.99 A; A=24-258.
DR PDB; 1P5V; X-ray; 1.70 A; A=24-258.
DR PDB; 1Z9S; X-ray; 2.20 A; A=24-258.
DR PDB; 2OS7; X-ray; 2.90 A; A/B/C/D/E/F=24-258.
DR PDB; 3DOS; X-ray; 2.40 A; A/D=24-258.
DR PDB; 3DPB; X-ray; 2.20 A; A=24-258.
DR PDB; 3DSN; X-ray; 2.20 A; A/D=24-258.
DR PDB; 4AY0; X-ray; 1.52 A; A/B=24-258.
DR PDB; 4AYF; X-ray; 2.07 A; A=24-258.
DR PDB; 4AZ8; X-ray; 2.65 A; A=24-258.
DR PDB; 4B0M; X-ray; 1.80 A; M=24-258.
DR PDBsum; 1P5U; -.
DR PDBsum; 1P5V; -.
DR PDBsum; 1Z9S; -.
DR PDBsum; 2OS7; -.
DR PDBsum; 3DOS; -.
DR PDBsum; 3DPB; -.
DR PDBsum; 3DSN; -.
DR PDBsum; 4AY0; -.
DR PDBsum; 4AYF; -.
DR PDBsum; 4AZ8; -.
DR PDBsum; 4B0M; -.
DR AlphaFoldDB; P26926; -.
DR SMR; P26926; -.
DR DIP; DIP-35244N; -.
DR IntAct; P26926; 3.
DR MINT; P26926; -.
DR DNASU; 1149242; -.
DR EnsemblBacteria; AAC82756; AAC82756; AAC82756.
DR EnsemblBacteria; AAS58716; AAS58716; YP_pMT084.
DR GeneID; 57977634; -.
DR KEGG; ype:YPMT1.82; -.
DR KEGG; ypk:caf1M.pl; -.
DR KEGG; ypm:YP_pMT084; -.
DR PATRIC; fig|214092.21.peg.210; -.
DR HOGENOM; CLU_070768_2_2_6; -.
DR OMA; LQWLCVK; -.
DR EvolutionaryTrace; P26926; -.
DR PRO; PR:P26926; -.
DR Proteomes; UP000000815; Plasmid pMT1 (pMT-1).
DR Proteomes; UP000001019; Plasmid pMT1.
DR Proteomes; UP000002490; Plasmid pMT-1.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008962; PapD-like_sf.
DR InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR Pfam; PF02753; PapD_C; 1.
DR Pfam; PF00345; PapD_N; 1.
DR PRINTS; PR00969; CHAPERONPILI.
DR SUPFAM; SSF49354; SSF49354; 1.
DR SUPFAM; SSF49584; SSF49584; 1.
DR PROSITE; PS00635; PILI_CHAPERONE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Disulfide bond; Immunoglobulin domain; Periplasm;
KW Plasmid; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..258
FT /note="Chaperone protein caf1M"
FT /id="PRO_0000009264"
FT DISULFID 121..160
FT /evidence="ECO:0000255"
FT CONFLICT 180
FT /note="N -> K (in Ref. 1; CAA43967)"
FT /evidence="ECO:0000305"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:2OS7"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2OS7"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:4AY0"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2OS7"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2OS7"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1P5V"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4AY0"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:4AY0"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4B0M"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4AY0"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2OS7"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:4AY0"
SQ SEQUENCE 258 AA; 28751 MW; 8049DCC1A80C7391 CRC64;
MILNRLSTLG IITFGMLSFA ANSAQPDIKF ASKEYGVTIG ESRIIYPLDA AGVMVSVKNT
QDYPVLIQSR IYDENKEKES EDPFVVTPPL FRLDAKQQNS LRIAQAGGVF PRDKESLKWL
CVKGIPPKDE DIWVDDATNK QKFNPDKDVG VFVQFAINNC IKLLVRPNEL KGTPIQFAEN
LSWKVDGGKL IAENPSPFYM NIGELTFGGK SIPSHYIPPK STWAFDLPKG LAGARNVSWR
IINDQGGLDR LYSKNVTL
