IBPB_ENT38
ID IBPB_ENT38 Reviewed; 142 AA.
AC A4W4S4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=Ent638_0014;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP58704.1; -; Genomic_DNA.
DR RefSeq; WP_011915282.1; NC_009436.1.
DR AlphaFoldDB; A4W4S4; -.
DR SMR; A4W4S4; -.
DR STRING; 399742.Ent638_0014; -.
DR EnsemblBacteria; ABP58704; ABP58704; Ent638_0014.
DR KEGG; ent:Ent638_0014; -.
DR eggNOG; COG0071; Bacteria.
DR HOGENOM; CLU_046737_4_2_6; -.
DR OMA; KESEYLH; -.
DR OrthoDB; 1523369at2; -.
DR Proteomes; UP000000230; 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..142
FT /note="Small heat shock protein IbpB"
FT /id="PRO_1000070882"
FT DOMAIN 26..137
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ SEQUENCE 142 AA; 15984 MW; 2892B584F02B6863 CRC64;
MRNHDLSPLL RQWIGFDKLA NALQSTAEHQ AFPPYNIEKS DDNHYRITLA LAGFRQDDLD
IQLEGTRLTV KGTPEKPETE TKWLHQGLVI QPFSLSFTLA DHMEVTGATF TNGLLHIDLT
RNVPEALAPQ RIAISDRPAL NS
