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Protein

Small heat shock protein IbpA

Gene

ibpA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • protein stabilization Source: UniProtKB-HAMAP
  • response to heat Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:EG11534-MONOMER.
ECOL316407:JW3664-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Small heat shock protein IbpA
Alternative name(s):
16 kDa heat shock protein A
Gene namesi
Name:ibpA
Synonyms:hslT, htpN
Ordered Locus Names:b3687, JW3664
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11534. ibpA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Small heat shock protein IbpAPRO_0000126017Add
BLAST

Proteomic databases

PaxDbiP0C054.
PRIDEiP0C054.

2D gel databases

SWISS-2DPAGEP0C054.

Expressioni

Inductioni

By heat shock.

Interactioni

Subunit structurei

Monomer. Forms homomultimers of about 100-150 subunits at optimal growth temperatures. Conformation changes to monomers at high temperatures or high ionic concentrations.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-550729,EBI-550729
ibpBP0C0583EBI-550729,EBI-552784

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262590. 160 interactions.
DIPiDIP-47849N.
IntActiP0C054. 45 interactions.
MINTiMINT-1219330.
STRINGi511145.b3687.

Structurei

3D structure databases

ProteinModelPortaliP0C054.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108ZNX. Bacteria.
COG0071. LUCA.
HOGENOMiHOG000251750.
InParanoidiP0C054.
KOiK04080.
OMAiTAHDNML.
OrthoDBiEOG65TRT6.
PhylomeDBiP0C054.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
HAMAPiMF_02000. HSP20_IbpA.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
IPR023728. HSP20_IbpA.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C054-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNFDLSPLY RSAIGFDRLF NHLENNQSQS NGGYPPYNVE LVDENHYRIA
60 70 80 90 100
IAVAGFAESE LEITAQDNLL VVKGAHADEQ KERTYLYQGI AERNFERKFQ
110 120 130
LAENIHVRGA NLVNGLLYID LERVIPEAKK PRRIEIN
Length:137
Mass (Da):15,774
Last modified:July 5, 2005 - v1
Checksum:iE7BB51421F5CEF3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94104 Genomic DNA. Translation: AAA24424.1.
L10328 Genomic DNA. Translation: AAA62039.1.
U00096 Genomic DNA. Translation: AAC76710.1.
AP009048 Genomic DNA. Translation: BAE77607.1.
PIRiA45245.
RefSeqiNP_418142.1. NC_000913.3.
WP_001243437.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76710; AAC76710; b3687.
BAE77607; BAE77607; BAE77607.
GeneIDi948200.
KEGGiecj:JW3664.
eco:b3687.
PATRICi32122867. VBIEscCol129921_3809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94104 Genomic DNA. Translation: AAA24424.1.
L10328 Genomic DNA. Translation: AAA62039.1.
U00096 Genomic DNA. Translation: AAC76710.1.
AP009048 Genomic DNA. Translation: BAE77607.1.
PIRiA45245.
RefSeqiNP_418142.1. NC_000913.3.
WP_001243437.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0C054.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262590. 160 interactions.
DIPiDIP-47849N.
IntActiP0C054. 45 interactions.
MINTiMINT-1219330.
STRINGi511145.b3687.

2D gel databases

SWISS-2DPAGEP0C054.

Proteomic databases

PaxDbiP0C054.
PRIDEiP0C054.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76710; AAC76710; b3687.
BAE77607; BAE77607; BAE77607.
GeneIDi948200.
KEGGiecj:JW3664.
eco:b3687.
PATRICi32122867. VBIEscCol129921_3809.

Organism-specific databases

EchoBASEiEB1496.
EcoGeneiEG11534. ibpA.

Phylogenomic databases

eggNOGiENOG4108ZNX. Bacteria.
COG0071. LUCA.
HOGENOMiHOG000251750.
InParanoidiP0C054.
KOiK04080.
OMAiTAHDNML.
OrthoDBiEOG65TRT6.
PhylomeDBiP0C054.

Enzyme and pathway databases

BioCyciEcoCyc:EG11534-MONOMER.
ECOL316407:JW3664-MONOMER.

Miscellaneous databases

PROiP0C054.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
HAMAPiMF_02000. HSP20_IbpA.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
IPR023728. HSP20_IbpA.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli."
    Allen S.P., Polazzi J.O., Gierse J., Easton A.M.
    J. Bacteriol. 174:6938-6947(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  6. "Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli."
    Kitagawa M., Matsumura Y., Tsuchido T.
    FEMS Microbiol. Lett. 184:165-171(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RESISTANCE TO OXIDATIVE STRESS.
  7. "The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock."
    Kuczynska-Wisnik D., Kedzierska S., Matuszewska E., Lund P., Taylor A., Lipinska B., Laskowska E.
    Microbiology 148:1757-1765(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants."
    Kitagawa M., Miyakawa M., Matsumura Y., Tsuchido T.
    Eur. J. Biochem. 269:2907-2917(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  9. "Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation."
    Mogk A., Deuerling E., Vorderwuelbecke S., Vierling E., Bukau B.
    Mol. Microbiol. 50:585-595(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE CLPB AND DNAK CHAPERONE SYSTEMS.
  10. "Aggregation of heat-shock-denatured, endogenous proteins and distribution of the IbpA/B and Fda marker-proteins in Escherichia coli WT and grpE280 cells."
    Laskowska E., Bohdanowicz J., Kuczynska-Wisnik D., Matuszewska E., Kedzierska S., Taylor A.
    Microbiology 150:247-259(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state."
    Matuszewska M., Kuczynska-Wisnik D., Laskowska E., Liberek K.
    J. Biol. Chem. 280:12292-12298(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IBPB.

Entry informationi

Entry nameiIBPA_ECOLI
AccessioniPrimary (citable) accession number: P0C054
Secondary accession number(s): P29209, Q2M7Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: January 20, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.