ID   IBPA_SALCH              Reviewed;         137 AA.
AC   Q57I24;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=SCH_3732;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX67638.1; -; Genomic_DNA.
DR   RefSeq; WP_001532742.1; NC_006905.1.
DR   AlphaFoldDB; Q57I24; -.
DR   SMR; Q57I24; -.
DR   EnsemblBacteria; AAX67638; AAX67638; SCH_3732.
DR   KEGG; sec:SCH_3732; -.
DR   HOGENOM; CLU_046737_4_2_6; -.
DR   OMA; TAHDNML; -.
DR   Proteomes; UP000000538; 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_0000126021"
FT   DOMAIN          28..137
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ   SEQUENCE   137 AA;  15750 MW;  13EF8A31032A3453 CRC64;
     MRNFDLSPLY RSAIGFDRLF NLLENNQSQS NGGYPPYNVE LVDENHYRIA IAVAGFAESE
     LEITAQDNLL VVKGAHADEQ KERTYLYQGI AERNFERKFQ LAENIHVRGA NLVNGLLYIE
     LERVIPEANK PRRIEIN