IBPB_ECO5E
ID IBPB_ECO5E Reviewed; 142 AA.
AC B5YX92;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=ECH74115_5118;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RX PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001164; ACI34651.1; -; Genomic_DNA.
DR RefSeq; WP_001243431.1; NC_011353.1.
DR AlphaFoldDB; B5YX92; -.
DR SMR; B5YX92; -.
DR GeneID; 67417681; -.
DR KEGG; ecf:ECH74115_5118; -.
DR HOGENOM; CLU_046737_4_2_6; -.
DR OMA; SGNEGYP; -.
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_1000189098"
FT DOMAIN 26..137
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ SEQUENCE 142 AA; 16093 MW; 7666BB1BDB8A673A CRC64;
MRNFDLSPLM RQWIGFDKLA NALQNAGESQ SFPPYNIEKS DDNHYRITLA LAGFRQEDLE
IQLEGTRLSV KGTPEQPKEE KKWLHQGLMN QPFSLSFTLA ENMEVSGATF VNGLLHIDLI
RNEPEPIAAQ RIAISERPAL NS