ID   IBPA_YERPS              Reviewed;         137 AA.
AC   Q663X0;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=YPTB3904;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH23142.1; -; Genomic_DNA.
DR   RefSeq; WP_002209636.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q663X0; -.
DR   SMR; Q663X0; -.
DR   EnsemblBacteria; CAH23142; CAH23142; YPTB3904.
DR   GeneID; 66843677; -.
DR   KEGG; ypo:BZ17_2677; -.
DR   KEGG; yps:YPTB3904; -.
DR   PATRIC; fig|273123.14.peg.2806; -.
DR   OMA; TAHDNML; -.
DR   Proteomes; UP000001011; 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_0000126027"
FT   DOMAIN          28..137
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ   SEQUENCE   137 AA;  15648 MW;  3DE2C401118C0C59 CRC64;
     MRNSDLAPLY RSAIGFDRLF NLLESGQNQS NGGYPPYNVE LVDENNYRIA IAVAGFAEQE
     LEITTQDNLL IVRGSHANEP AQRTYLYQGI AERNFERKFQ LAEHIKIKGA NLVNGLLYID
     LERLVPESLK PRRIEIK