Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Small heat shock protein IbpB

Gene

ibpB

Organism
Escherichia coli (strain K12 / DH10B)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Associates with aggregated proteins, together with IbpA, 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.UniRule annotation

Keywordsi

Molecular functionChaperone
Biological processStress response

Names & Taxonomyi

Protein namesi
Recommended name:
Small heat shock protein IbpBUniRule annotation
Alternative name(s):
16 kDa heat shock protein BUniRule annotation
Gene namesi
Name:ibpBUniRule annotation
Ordered Locus Names:ECDH10B_3872
OrganismiEscherichia coli (strain K12 / DH10B)
Taxonomic identifieri316385 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001891021 – 142Small heat shock protein IbpBAdd BLAST142

Interactioni

Subunit structurei

Homodimer. Forms homomultimers of about 100-150 subunits at optimal growth temperatures. Conformation changes to oligomers at high temperatures or high ionic concentrations. The decrease in size of the multimers is accompanied by an increase in chaperone activity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB1X9B6
SMRiB1X9B6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 137sHSPPROSITE-ProRule annotationAdd BLAST112

Domaini

The N- and C-terminal flexible termini are involved in oligomerization and in the binding of non-native substrate proteins, and are essential for chaperone activity.UniRule annotation

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108SHS Bacteria
COG0071 LUCA
HOGENOMiHOG000251750
KOiK04081
OMAiKASDGYP

Family and domain databases

CDDicd06470 ACD_IbpA-B_like, 1 hit
Gene3Di2.60.40.790, 1 hit
HAMAPiMF_02001 HSP20_IbpB, 1 hit
InterProiView protein in InterPro
IPR002068 A-crystallin/Hsp20_dom
IPR037913 ACD_IbpA/B
IPR031107 HSP20
IPR008978 HSP20-like_chaperone
IPR022848 HSP20_IbpB
PANTHERiPTHR11527 PTHR11527, 1 hit
PfamiView protein in Pfam
PF00011 HSP20, 1 hit
SUPFAMiSSF49764 SSF49764, 1 hit
PROSITEiView protein in PROSITE
PS01031 SHSP, 1 hit

Sequencei

Sequence statusi: Complete.

B1X9B6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNFDLSPLM RQWIGFDKLA NALQNAGESQ SFPPYNIEKS DDNHYRITLA
60 70 80 90 100
LAGFRQEDLE IQLEGTRLSV KGTPEQPKEE KKWLHQGLMN QPFSLSFTLA
110 120 130 140
ENMEVSGATF VNGLLHIDLI RNEPEPIAAQ RIAISERPAL NS
Length:142
Mass (Da):16,093
Last modified:May 20, 2008 - v1
Checksum:i7666BB1BDB8A673A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000948 Genomic DNA Translation: ACB04732.1
RefSeqiWP_001243431.1, NC_010473.1

Genome annotation databases

EnsemblBacteriaiACB04732; ACB04732; ECDH10B_3872
KEGGiecd:ECDH10B_3872

Similar proteinsi

Entry informationi

Entry nameiIBPB_ECODH
AccessioniPrimary (citable) accession number: B1X9B6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 20, 2008
Last modified: April 25, 2018
This is version 59 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health