IBPA_ESCF3
ID IBPA_ESCF3 Reviewed; 137 AA.
AC B7LK29;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=EFER_3982;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ91416.1; -; Genomic_DNA.
DR RefSeq; WP_001243437.1; NC_011740.1.
DR AlphaFoldDB; B7LK29; -.
DR SMR; B7LK29; -.
DR EnsemblBacteria; CAQ91416; CAQ91416; EFER_3982.
DR GeneID; 67417682; -.
DR KEGG; efe:EFER_3982; -.
DR HOGENOM; CLU_046737_4_2_6; -.
DR OMA; TAHDNML; -.
DR OrthoDB; 1523369at2; -.
DR BioCyc; EFER585054:EFER_RS19905-MON; -.
DR Proteomes; UP000000745; 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_1000189087"
FT DOMAIN 28..137
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ SEQUENCE 137 AA; 15774 MW; E7BB51421F5CEF3E CRC64;
MRNFDLSPLY RSAIGFDRLF NHLENNQSQS NGGYPPYNVE LVDENHYRIA IAVAGFAESE
LEITAQDNLL VVKGAHADEQ KERTYLYQGI AERNFERKFQ LAENIHVRGA NLVNGLLYID
LERVIPEAKK PRRIEIN