ID   IBPB_CITK8              Reviewed;         142 AA.
AC   A8ACJ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=CKO_00033;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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; CP000822; ABV11212.1; -; Genomic_DNA.
DR   RefSeq; WP_012000793.1; NC_009792.1.
DR   AlphaFoldDB; A8ACJ9; -.
DR   SMR; A8ACJ9; -.
DR   STRING; 290338.CKO_00033; -.
DR   EnsemblBacteria; ABV11212; ABV11212; CKO_00033.
DR   GeneID; 45134341; -.
DR   KEGG; cko:CKO_00033; -.
DR   HOGENOM; CLU_046737_4_2_6; -.
DR   OMA; SGNEGYP; -.
DR   OrthoDB; 1523369at2; -.
DR   Proteomes; UP000008148; 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..142
FT                   /note="Small heat shock protein IbpB"
FT                   /id="PRO_1000022030"
FT   DOMAIN          26..137
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ   SEQUENCE   142 AA;  16023 MW;  CB2445B66EEB184D CRC64;
     MRNYDLSPLL RQWIGFDKLA NALQNTGESQ SFPPYNIEKS DDNHYRITLA LAGFRQEDLD
     IQLEGTRLTV KGTPAQPEKE IKWLHQGLVT QPFSLSFTLA ENMEVSGATF TNGLLHIDLT
     RNEPETIAPQ RIAISERPAL NS