IBPB_ECOLI
ID IBPB_ECOLI Reviewed; 142 AA.
AC P0C058; P29210; P76733; Q2M7Z8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Small heat shock protein IbpB;
DE AltName: Full=16 kDa heat shock protein B;
GN Name=ibpB; Synonyms=hslS, htpE; OrderedLocusNames=b3686, JW3663;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND INDUCTION.
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 FUNCTION.
RX PubMed=9556585; DOI=10.1074/jbc.273.18.11032;
RA Veinger L., Diamant S., Buchner J., Goloubinoff P.;
RT "The small heat-shock protein IbpB from Escherichia coli stabilizes stress-
RT denatured proteins for subsequent refolding by a multichaperone network.";
RL J. Biol. Chem. 273:11032-11037(1998).
RN [7]
RP CHARACTERIZATION, AND SUBUNIT.
RX PubMed=10187768; DOI=10.1074/jbc.274.15.9937;
RA Shearstone J.R., Baneyx F.;
RT "Biochemical characterization of the small heat shock protein IbpB from
RT Escherichia coli.";
RL J. Biol. Chem. 274:9937-9945(1999).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
RP INTERACTION WITH IBPBA.
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).
RN [14]
RP SUBUNIT, AND DOMAIN.
RX PubMed=15769476; DOI=10.1016/j.jmb.2005.01.029;
RA Jiao W., Qian M., Li P., Zhao L., Chang Z.;
RT "The essential role of the flexible termini in the temperature-
RT responsiveness of the oligomeric state and chaperone-like activity for the
RT polydisperse small heat shock protein IbpB from Escherichia coli.";
RL J. Mol. Biol. 347:871-884(2005).
CC -!- FUNCTION: Associates with aggregated proteins, together with IbpA, 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 ECO:0000269|PubMed:9556585}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable up to 50 degrees Celsius.;
CC -!- SUBUNIT: Homodimer. Forms homomultimers of about 100-150 subunits at
CC optimal growth temperatures. Conformation changes to oligomers at high
CC temperatures or high ionic concentrations. The decrease in size of the
CC multimers is accompanied by an increase in chaperone activity.
CC {ECO:0000269|PubMed:10187768, ECO:0000269|PubMed:12071954,
CC ECO:0000269|PubMed:15769476}.
CC -!- INTERACTION:
CC P0C058; P0C054: ibpA; NbExp=5; IntAct=EBI-552784, EBI-550729;
CC P0C058; P0C058: ibpB; NbExp=3; IntAct=EBI-552784, EBI-552784;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14702418}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:1356969}.
CC -!- DOMAIN: The N- and C-terminal flexible termini are involved in
CC oligomerization and in the binding of non-native substrate proteins,
CC and are essential for chaperone activity.
CC {ECO:0000269|PubMed:15769476}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62038.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M94104; AAA24425.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62038.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76709.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77608.1; -; Genomic_DNA.
DR RefSeq; NP_418141.2; NC_000913.3.
DR RefSeq; WP_001243431.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P0C058; -.
DR SMR; P0C058; -.
DR BioGRID; 4260809; 224.
DR BioGRID; 852497; 1.
DR DIP; DIP-48244N; -.
DR IntAct; P0C058; 11.
DR MINT; P0C058; -.
DR STRING; 511145.b3686; -.
DR PaxDb; P0C058; -.
DR PRIDE; P0C058; -.
DR EnsemblBacteria; AAC76709; AAC76709; b3686.
DR EnsemblBacteria; BAE77608; BAE77608; BAE77608.
DR GeneID; 67417681; -.
DR GeneID; 948192; -.
DR KEGG; ecj:JW3663; -.
DR KEGG; eco:b3686; -.
DR PATRIC; fig|511145.12.peg.3808; -.
DR EchoBASE; EB1497; -.
DR eggNOG; COG0071; Bacteria.
DR HOGENOM; CLU_046737_4_2_6; -.
DR InParanoid; P0C058; -.
DR OMA; SGNEGYP; -.
DR PhylomeDB; P0C058; -.
DR BioCyc; EcoCyc:EG11535-MON; -.
DR PRO; PR:P0C058; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0050821; P:protein stabilization; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:1990169; P:stress response to copper ion; IMP:EcoCyc.
DR CDD; cd06470; ACD_IbpA-B_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR HAMAP; MF_02001; HSP20_IbpB; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037913; ACD_IbpA/B.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR022848; HSP20_IbpB.
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..142
FT /note="Small heat shock protein IbpB"
FT /id="PRO_0000126028"
FT DOMAIN 26..137
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ SEQUENCE 142 AA; 16093 MW; 7666BB1BDB8A673A CRC64;
MRNFDLSPLM RQWIGFDKLA NALQNAGESQ SFPPYNIEKS DDNHYRITLA LAGFRQEDLE
IQLEGTRLSV KGTPEQPKEE KKWLHQGLMN QPFSLSFTLA ENMEVSGATF VNGLLHIDLI
RNEPEPIAAQ RIAISERPAL NS
