IBPB_YERPE
ID IBPB_YERPE Reviewed; 154 AA.
AC Q8Z9V6; Q0W9V0; Q74PC5; Q8CZG5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Small heat shock protein IbpB {ECO:0000255|HAMAP-Rule:MF_02001};
DE AltName: Full=16 kDa heat shock protein B {ECO:0000255|HAMAP-Rule:MF_02001};
GN Name=ibpB {ECO:0000255|HAMAP-Rule:MF_02001};
GN OrderedLocusNames=YPO4084, y4101, YP_3993;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
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).
CC -!- FUNCTION: Associates with aggregated proteins, together with IbpA, to
CC stabilize and protect them from irreversible denaturation and extensive
CC proteolysis during heat shock and oxidative stress. Aggregated proteins
CC bound to the IbpAB complex are more efficiently refolded and
CC reactivated by the ATP-dependent chaperone systems ClpB and
CC DnaK/DnaJ/GrpE. Its activity is ATP-independent. {ECO:0000255|HAMAP-
CC Rule:MF_02001}.
CC -!- SUBUNIT: Homodimer. Forms homomultimers of about 100-150 subunits at
CC optimal growth temperatures. Conformation changes to oligomers at high
CC temperatures or high ionic concentrations. The decrease in size of the
CC multimers is accompanied by an increase in chaperone activity.
CC {ECO:0000255|HAMAP-Rule:MF_02001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02001}.
CC -!- DOMAIN: The N- and C-terminal flexible termini are involved in
CC oligomerization and in the binding of non-native substrate proteins,
CC and are essential for chaperone activity. {ECO:0000255|HAMAP-
CC Rule:MF_02001}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|HAMAP-Rule:MF_02001, ECO:0000255|PROSITE-
CC ProRule:PRU00285}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM87644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS64133.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL22654.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87644.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS64133.1; ALT_INIT; Genomic_DNA.
DR PIR; AC0496; AC0496.
DR RefSeq; WP_002209635.1; NZ_WUCM01000035.1.
DR RefSeq; YP_002348938.1; NC_003143.1.
DR AlphaFoldDB; Q8Z9V6; -.
DR SMR; Q8Z9V6; -.
DR STRING; 214092.YPO4084; -.
DR PaxDb; Q8Z9V6; -.
DR EnsemblBacteria; AAM87644; AAM87644; y4101.
DR EnsemblBacteria; AAS64133; AAS64133; YP_3993.
DR GeneID; 66843676; -.
DR KEGG; ype:YPO4084; -.
DR KEGG; ypk:y4101; -.
DR KEGG; ypm:YP_3993; -.
DR PATRIC; fig|214092.21.peg.4625; -.
DR eggNOG; COG0071; Bacteria.
DR HOGENOM; CLU_046737_4_2_6; -.
DR OMA; KESEYLH; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050821; P:protein stabilization; IEA:UniProtKB-UniRule.
DR CDD; cd06470; ACD_IbpA-B_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR HAMAP; MF_02001; HSP20_IbpB; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037913; ACD_IbpA/B.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR022848; HSP20_IbpB.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..154
FT /note="Small heat shock protein IbpB"
FT /id="PRO_0000126037"
FT DOMAIN 26..137
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ SEQUENCE 154 AA; 17489 MW; F03AD1D39FE6A0C4 CRC64;
MRNYDLSPLL RQWIGFDKLA STMQGGQEPQ GFPPYNIEKT DDNHYRISLA LAGFKQSELD
IEVEGPRLTV RGKPTPVEKQ VEYLHQGLVR KEFSLTFTLA EHLNVDNAQF ENGLLHIDLL
RQVPEALQPQ RIAIGSATPQ ERQVLESPEA PDQQ
