ID IBPA_SHIFL Reviewed; 137 AA.
AC P0C057; P29209;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
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};
GN OrderedLocusNames=SF3776, S3994;
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45218.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18979.1; -; Genomic_DNA.
DR RefSeq; NP_709511.2; NC_004337.2.
DR RefSeq; WP_001243437.1; NZ_WPGW01000019.1.
DR AlphaFoldDB; P0C057; -.
DR SMR; P0C057; -.
DR STRING; 198214.SF3776; -.
DR PaxDb; 198214-SF3776; -.
DR GeneID; 1026089; -.
DR GeneID; 83578767; -.
DR KEGG; sfl:SF3776; -.
DR KEGG; sfx:S3994; -.
DR PATRIC; fig|198214.7.peg.4457; -.
DR HOGENOM; CLU_046737_4_2_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 PANTHER; PTHR47062; -; 1.
DR PANTHER; PTHR47062:SF1; SMALL HEAT SHOCK PROTEIN IBPA; 1.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..137
FT /note="Small heat shock protein IbpA"
FT /id="PRO_0000126025"
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
//
