ID   IBPB_KLEP3              Reviewed;         142 AA.
AC   B5XT61;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=KPK_0011;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI10740.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XT61; -.
DR   SMR; B5XT61; -.
DR   EnsemblBacteria; ACI10740; ACI10740; KPK_0011.
DR   KEGG; kpe:KPK_0011; -.
DR   HOGENOM; CLU_046737_4_2_6; -.
DR   OMA; SGNEGYP; -.
DR   OrthoDB; 1523369at2; -.
DR   Proteomes; UP000001734; 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_1000189106"
FT   DOMAIN          26..137
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ   SEQUENCE   142 AA;  15969 MW;  49E0D4D31A3B9341 CRC64;
     MRNYDLSPLL RQWIGFDKLA NALQTAGESQ SFPPYNIEKS DDNHYRITLA LAGFRQEDLD
     IQLEGTRLVV KGTPQQPEKE TTWLHQGLVS QAFSLSFTLA DNMEVSGATF TNGLLHIDLT
     RNEPEQIAPQ RIAISERPAL NS