ID   IBPA_PECCP              Reviewed;         137 AA.
AC   C6DGL0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=PC1_0034;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT11097.1; -; Genomic_DNA.
DR   RefSeq; WP_005976748.1; NC_012917.1.
DR   AlphaFoldDB; C6DGL0; -.
DR   SMR; C6DGL0; -.
DR   STRING; 561230.PC1_0034; -.
DR   EnsemblBacteria; ACT11097; ACT11097; PC1_0034.
DR   GeneID; 51387471; -.
DR   GeneID; 57312263; -.
DR   GeneID; 61345942; -.
DR   GeneID; 66800323; -.
DR   KEGG; pct:PC1_0034; -.
DR   eggNOG; COG0071; Bacteria.
DR   HOGENOM; CLU_046737_4_2_6; -.
DR   OMA; TAHDNML; -.
DR   OrthoDB; 1523369at2; -.
DR   Proteomes; UP000002736; 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_1000216228"
FT   DOMAIN          28..137
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ   SEQUENCE   137 AA;  15620 MW;  E7C39B4D27E0A54B CRC64;
     MRNPDFSPLY RSAIGFDRLF NLLETGQTQS NGGYPPYNVE LVDENQYRIA IAVAGFAEQE
     LDITAHDNLL IVKGAHAGEQ VARNYLYQGI AERNFERKFQ LAEHIQVKGA NLENGLLYID
     LERIVPEAMK PRRIEIK