IBPB_PECCP
ID IBPB_PECCP Reviewed; 149 AA.
AC C6DGL1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=PC1_0035;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT11098.1; -; Genomic_DNA.
DR RefSeq; WP_012772780.1; NC_012917.1.
DR AlphaFoldDB; C6DGL1; -.
DR SMR; C6DGL1; -.
DR STRING; 561230.PC1_0035; -.
DR PRIDE; C6DGL1; -.
DR EnsemblBacteria; ACT11098; ACT11098; PC1_0035.
DR KEGG; pct:PC1_0035; -.
DR eggNOG; COG0071; Bacteria.
DR HOGENOM; CLU_046737_4_2_6; -.
DR OMA; KESEYLH; -.
DR OrthoDB; 1523369at2; -.
DR Proteomes; UP000002736; 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; Stress response.
FT CHAIN 1..149
FT /note="Small heat shock protein IbpB"
FT /id="PRO_1000216230"
FT DOMAIN 26..137
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ SEQUENCE 149 AA; 16699 MW; 5C645C91411B7AF7 CRC64;
MRNYDLSPLL RQWIGFDKLA SSMQGSQEPI DFPPYNIEKK DDNHYRITLA LAGFRQSDLD
IEVEGPRLTV KGSPAPTEKA VEYLHQGLVF KPFTLSFTLA EHLHVSDAHF ENGLLHIDLV
RDVPEALQPQ RIAIGGGRPA LNQQPAEDA
