IBPB_YERPY
ID IBPB_YERPY Reviewed; 154 AA.
AC B1JGZ6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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}; OrderedLocusNames=YPK_0012;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000950; ACA66326.1; -; Genomic_DNA.
DR RefSeq; WP_002209635.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JGZ6; -.
DR SMR; B1JGZ6; -.
DR EnsemblBacteria; ACA66326; ACA66326; YPK_0012.
DR GeneID; 66843676; -.
DR KEGG; ypy:YPK_0012; -.
DR PATRIC; fig|502800.11.peg.614; -.
DR OMA; KESEYLH; -.
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; Stress response.
FT CHAIN 1..154
FT /note="Small heat shock protein IbpB"
FT /id="PRO_1000189117"
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
