IBPA_ECOLI
ID IBPA_ECOLI Reviewed; 137 AA.
AC P0C054; P29209; Q2M7Z9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Small heat shock protein IbpA;
DE AltName: Full=16 kDa heat shock protein A;
GN Name=ibpA; Synonyms=hslT, htpN; OrderedLocusNames=b3687, JW3664;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1356969; DOI=10.1128/jb.174.21.6938-6947.1992;
RA Allen S.P., Polazzi J.O., Gierse J., Easton A.M.;
RT "Two novel heat shock genes encoding proteins produced in response to
RT heterologous protein expression in Escherichia coli.";
RL J. Bacteriol. 174:6938-6947(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [6]
RP INVOLVEMENT IN RESISTANCE TO OXIDATIVE STRESS.
RX PubMed=10713416; DOI=10.1111/j.1574-6968.2000.tb09009.x;
RA Kitagawa M., Matsumura Y., Tsuchido T.;
RT "Small heat shock proteins, IbpA and IbpB, are involved in resistances to
RT heat and superoxide stresses in Escherichia coli.";
RL FEMS Microbiol. Lett. 184:165-171(2000).
RN [7]
RP FUNCTION.
RX PubMed=12055295; DOI=10.1099/00221287-148-6-1757;
RA Kuczynska-Wisnik D., Kedzierska S., Matuszewska E., Lund P., Taylor A.,
RA Lipinska B., Laskowska E.;
RT "The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the
RT aggregation of endogenous proteins denatured in vivo during extreme heat
RT shock.";
RL Microbiology 148:1757-1765(2002).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12071954; DOI=10.1046/j.1432-1033.2002.02958.x;
RA Kitagawa M., Miyakawa M., Matsumura Y., Tsuchido T.;
RT "Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes
RT from inactivation by heat and oxidants.";
RL Eur. J. Biochem. 269:2907-2917(2002).
RN [9]
RP INTERACTION WITH THE CLPB AND DNAK CHAPERONE SYSTEMS.
RX PubMed=14617181; DOI=10.1046/j.1365-2958.2003.03710.x;
RA Mogk A., Deuerling E., Vorderwuelbecke S., Vierling E., Bukau B.;
RT "Small heat shock proteins, ClpB and the DnaK system form a functional
RT triade in reversing protein aggregation.";
RL Mol. Microbiol. 50:585-595(2003).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=14702418; DOI=10.1099/mic.0.26470-0;
RA Laskowska E., Bohdanowicz J., Kuczynska-Wisnik D., Matuszewska E.,
RA Kedzierska S., Taylor A.;
RT "Aggregation of heat-shock-denatured, endogenous proteins and distribution
RT of the IbpA/B and Fda marker-proteins in Escherichia coli WT and grpE280
RT cells.";
RL Microbiology 150:247-259(2004).
RN [11]
RP INTERACTION WITH IBPB.
RX PubMed=15665332; DOI=10.1074/jbc.m412706200;
RA Matuszewska M., Kuczynska-Wisnik D., Laskowska E., Liberek K.;
RT "The small heat shock protein IbpA of Escherichia coli cooperates with IbpB
RT in stabilization of thermally aggregated proteins in a disaggregation
RT competent state.";
RL J. Biol. Chem. 280:12292-12298(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.
CC {ECO:0000269|PubMed:12055295, ECO:0000269|PubMed:12071954}.
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.
CC {ECO:0000269|PubMed:12071954}.
CC -!- INTERACTION:
CC P0C054; P0C054: ibpA; NbExp=3; IntAct=EBI-550729, EBI-550729;
CC P0C054; P0C058: ibpB; NbExp=5; IntAct=EBI-550729, EBI-552784;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14702418}.
CC -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285, ECO:0000305}.
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DR EMBL; M94104; AAA24424.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62039.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76710.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77607.1; -; Genomic_DNA.
DR PIR; A45245; A45245.
DR RefSeq; NP_418142.1; NC_000913.3.
DR RefSeq; WP_001243437.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P0C054; -.
DR SMR; P0C054; -.
DR BioGRID; 4262590; 160.
DR DIP; DIP-47849N; -.
DR IntAct; P0C054; 50.
DR MINT; P0C054; -.
DR STRING; 511145.b3687; -.
DR SWISS-2DPAGE; P0C054; -.
DR jPOST; P0C054; -.
DR PaxDb; P0C054; -.
DR PRIDE; P0C054; -.
DR EnsemblBacteria; AAC76710; AAC76710; b3687.
DR EnsemblBacteria; BAE77607; BAE77607; BAE77607.
DR GeneID; 67417682; -.
DR GeneID; 948200; -.
DR KEGG; ecj:JW3664; -.
DR KEGG; eco:b3687; -.
DR PATRIC; fig|511145.12.peg.3809; -.
DR EchoBASE; EB1496; -.
DR eggNOG; COG0071; Bacteria.
DR HOGENOM; CLU_046737_4_2_6; -.
DR InParanoid; P0C054; -.
DR OMA; TAHDNML; -.
DR PhylomeDB; P0C054; -.
DR BioCyc; EcoCyc:EG11534-MON; -.
DR PRO; PR:P0C054; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:EcoCyc.
DR GO; GO:0017148; P:negative regulation of translation; IDA:EcoCyc.
DR GO; GO:0050821; P:protein stabilization; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Stress response.
FT CHAIN 1..137
FT /note="Small heat shock protein IbpA"
FT /id="PRO_0000126017"
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
