ID   IBPA_KLEP3              Reviewed;         137 AA.
AC   B5XT60;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Small heat shock protein IbpA {ECO:0000255|HAMAP-Rule:MF_02000};
DE   AltName: Full=16 kDa heat shock protein A {ECO:0000255|HAMAP-Rule:MF_02000};
GN   Name=ibpA {ECO:0000255|HAMAP-Rule:MF_02000}; OrderedLocusNames=KPK_0010;
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 IbpB, 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_02000}.
CC   -!- SUBUNIT: Monomer. Forms homomultimers of about 100-150 subunits at
CC       optimal growth temperatures. Conformation changes to monomers at high
CC       temperatures or high ionic concentrations. {ECO:0000255|HAMAP-
CC       Rule:MF_02000}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02000}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|HAMAP-Rule:MF_02000, ECO:0000255|PROSITE-
CC       ProRule:PRU00285}.
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DR   EMBL; CP000964; ACI09975.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XT60; -.
DR   SMR; B5XT60; -.
DR   EnsemblBacteria; ACI09975; ACI09975; KPK_0010.
DR   KEGG; kpe:KPK_0010; -.
DR   HOGENOM; CLU_046737_4_2_6; -.
DR   OMA; TAHDNML; -.
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_02000; HSP20_IbpA; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR037913; ACD_IbpA/B.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR023728; HSP20_IbpA.
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..137
FT                   /note="Small heat shock protein IbpA"
FT                   /id="PRO_1000189088"
FT   DOMAIN          28..137
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ   SEQUENCE   137 AA;  15706 MW;  13EE43C69638B3C6 CRC64;
     MRNFDLSPLY RSAIGFDRLF NLLENNQSQS NGGYPPYNVE LVDENHYRIA IAVAGFAESE
     LEITAQDNLL IVKGAHAAEQ KERTYLYQGI AERNFERKFQ LAENIHVRGA NLVNGLLYID
     LERVIPEANK PRRIEIN