YSCB_YERPE
ID YSCB_YERPE Reviewed; 137 AA.
AC Q56973;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Chaperone protein YscB;
DE AltName: Full=Yop proteins translocation protein B;
GN Name=yscB; OrderedLocusNames=YPCD1.51, y5027, y0030, YP_pCD32;
OS Yersinia pestis.
OG Plasmid pCD1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=1624469; DOI=10.1128/jb.174.14.4820-4828.1992;
RA Haddix P.L., Straley S.C.;
RT "Structure and regulation of the Yersinia pestis yscBCDEF operon.";
RL J. Bacteriol. 174:4820-4828(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9746557; DOI=10.1128/iai.66.10.4611-4623.1998;
RA Perry R.D., Straley S.C., Fetherston J.D., Rose D.J., Gregor J.,
RA Blattner F.R.;
RT "DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of
RT Yersinia pestis KIM5.";
RL Infect. Immun. 66:4611-4623(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
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;
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;
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).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=KIM5 / Biovar Mediaevalis, and KIM8;
RX PubMed=9733695; DOI=10.1128/jb.180.18.4912-4921.1998;
RA Jackson M.W., Day J.B., Plano G.V.;
RT "YscB of Yersinia pestis functions as a specific chaperone for YopN.";
RL J. Bacteriol. 180:4912-4921(1998).
RN [7]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=KIM5 / Biovar Mediaevalis, and KIM8;
RX PubMed=10094626; DOI=10.1046/j.1365-2958.1998.01110.x;
RA Day J.B., Plano G.V.;
RT "A complex composed of SycN and YscB functions as a specific chaperone for
RT YopN in Yersinia pestis.";
RL Mol. Microbiol. 30:777-788(1998).
RN [8]
RP FUNCTION.
RC STRAIN=KIM5 / Biovar Mediaevalis, and KIM8;
RX PubMed=12535078; DOI=10.1046/j.1365-2958.2003.03343.x;
RA Day J.B., Ferracci F., Plano G.V.;
RT "Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis
RT yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a
RT phosphorylatable peptide tag and phosphospecific antibodies.";
RL Mol. Microbiol. 47:807-823(2003).
CC -!- FUNCTION: Functions as a specific chaperone for YopN. It could
CC facilitate the secretion and the subsequent translocation of YopN.
CC {ECO:0000269|PubMed:10094626, ECO:0000269|PubMed:12535078,
CC ECO:0000269|PubMed:9733695}.
CC -!- SUBUNIT: Interacts with SycN to form a complex which specifically binds
CC to YopN. {ECO:0000269|PubMed:10094626}.
CC -!- INTERACTION:
CC Q56973; Q9NSC5: HOMER3; Xeno; NbExp=2; IntAct=EBI-20592268, EBI-748420;
CC Q56973; O15162: PLSCR1; Xeno; NbExp=2; IntAct=EBI-20592268, EBI-740019;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9733695}. Cell
CC inner membrane {ECO:0000269|PubMed:9733695}; Peripheral membrane
CC protein {ECO:0000269|PubMed:9733695}. Note=Not exported across the
CC inner membrane.
CC -!- INDUCTION: Transcription is induced at 37 degrees Celsius but down-
CC regulated at this temperature by calcium. {ECO:0000269|PubMed:1624469}.
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DR EMBL; M83225; AAA27637.1; -; Genomic_DNA.
DR EMBL; AF074612; AAC69829.1; -; Genomic_DNA.
DR EMBL; AF053946; AAC62553.1; -; Genomic_DNA.
DR EMBL; AL117189; CAB54928.1; -; Genomic_DNA.
DR EMBL; AE017043; AAS58551.1; -; Genomic_DNA.
DR PIR; T43574; T43574.
DR RefSeq; NP_395185.1; NC_003131.1.
DR RefSeq; NP_857731.1; NC_004836.1.
DR RefSeq; NP_857926.1; NC_004839.1.
DR RefSeq; WP_002212925.1; NZ_WUCM01000070.1.
DR PDB; 1XKP; X-ray; 1.70 A; C=1-137.
DR PDBsum; 1XKP; -.
DR AlphaFoldDB; Q56973; -.
DR SMR; Q56973; -.
DR IntAct; Q56973; 4.
DR MINT; Q56973; -.
DR STRING; 214092.5832471; -.
DR DNASU; 1149290; -.
DR EnsemblBacteria; AAS58551; AAS58551; YP_pCD32.
DR GeneID; 66841097; -.
DR KEGG; ype:YPCD1.51; -.
DR KEGG; ypm:YP_pCD32; -.
DR PATRIC; fig|214092.21.peg.60; -.
DR eggNOG; ENOG5032ZXD; Bacteria.
DR HOGENOM; CLU_154680_0_0_6; -.
DR OMA; SYHLRID; -.
DR EvolutionaryTrace; Q56973; -.
DR Proteomes; UP000000815; Plasmid pCD1.
DR Proteomes; UP000001019; Plasmid pCD1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR InterPro; IPR013353; T3SS_YscB.
DR InterPro; IPR010261; Tir_chaperone.
DR Pfam; PF05932; CesT; 1.
DR TIGRFAMs; TIGR02513; type_III_yscB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chaperone; Cytoplasm;
KW Membrane; Plasmid; Reference proteome.
FT CHAIN 1..137
FT /note="Chaperone protein YscB"
FT /id="PRO_0000066478"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:1XKP"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1XKP"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:1XKP"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1XKP"
SQ SEQUENCE 137 AA; 15409 MW; 4526D6C24E9C288A CRC64;
MQNLLKNLAA SLGRKPFVAD KQGVYRLTID KHLVMLAPHG SELVLRTPID APMLREGNNV
NVTLLRSLMQ QALAWAKRYP QTLVLDDCGQ LVLEARLRLQ ELDTHGLQEV INKQLALLEH
LIPQLTPFSV ASRVGWN
