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Protein

10 kDa chaperonin

Gene

groS

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

Functioni

Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • chaperone mediated protein folding requiring cofactor Source: EcoCyc
  • protein folding Source: CACAO
  • response to heat Source: EcoliWiki
  • response to unfolded protein Source: GO_Central
  • virion assembly Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciEcoCyc:EG10600-MONOMER.
ECOL316407:JW4102-MONOMER.
MetaCyc:EG10600-MONOMER.
SABIO-RKP0A6F9.

Names & Taxonomyi

Protein namesi
Recommended name:
10 kDa chaperonin
Alternative name(s):
GroES protein
Protein Cpn10
Gene namesi
Name:groS
Synonyms:groES, mopB
Ordered Locus Names:b4142, JW4102
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10600. groS.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase; polar localization depends on the minCDE operon. Foci form near midcell.

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • GroEL-GroES complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001747461 – 9710 kDa chaperoninAdd BLAST97

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34N6-succinyllysine1 Publication1

Proteomic databases

EPDiP0A6F9.
PaxDbiP0A6F9.
PRIDEiP0A6F9.

2D gel databases

SWISS-2DPAGEP0A6F9.

Interactioni

Subunit structurei

Heptamer of 7 subunits arranged in a ring.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-369169,EBI-369169
groLP0A6F525EBI-369169,EBI-543750

GO - Molecular functioni

  • chaperone binding Source: GO_Central
  • identical protein binding Source: EcoCyc
  • unfolded protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi4262198. 133 interactors.
DIPiDIP-9835N.
IntActiP0A6F9. 28 interactors.
MINTiMINT-5232475.
STRINGi511145.b4142.

Structurei

Secondary structure

197
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Beta strandi7 – 14Combined sources8
Turni20 – 23Combined sources4
Beta strandi37 – 43Combined sources7
Beta strandi45 – 47Combined sources3
Beta strandi51 – 53Combined sources3
Beta strandi64 – 67Combined sources4
Beta strandi74 – 78Combined sources5
Beta strandi81 – 87Combined sources7
Helixi88 – 90Combined sources3
Beta strandi91 – 96Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AONX-ray3.00O/P/Q/R/S/T/U1-97[»]
1EGSNMR-A19-27[»]
1GRUelectron microscopy12.50O/P/Q/R/S/T/U1-97[»]
1PCQX-ray2.81O/P/Q/R/S/T/U1-97[»]
1PF9X-ray2.99O/P/Q/R/S/T/U1-97[»]
1SVTX-ray2.81O/P/Q/R/S/T/U1-97[»]
1SX4X-ray3.00O/P/Q/R/S/T/U1-97[»]
2C7Celectron microscopy7.70O/P/Q/R/S/T/U1-97[»]
2C7Delectron microscopy8.70O/P/Q/R/S/T/U1-97[»]
3WVLX-ray3.79O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b1-97[»]
3ZPZelectron microscopy8.90O/P/Q/R/S/T/U1-97[»]
3ZQ0electron microscopy9.20O/P/Q/R/S/T/U1-97[»]
3ZQ1electron microscopy15.90O/P/Q/R/S/T/U1-97[»]
ProteinModelPortaliP0A6F9.
SMRiP0A6F9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6F9.

Family & Domainsi

Sequence similaritiesi

Belongs to the GroES chaperonin family.Curated

Phylogenomic databases

eggNOGiENOG4105K5Y. Bacteria.
COG0234. LUCA.
HOGENOMiHOG000133897.
InParanoidiP0A6F9.
KOiK04078.
OMAiVMGENEI.
PhylomeDBiP0A6F9.

Family and domain databases

CDDicd00320. cpn10. 1 hit.
Gene3Di2.30.33.40. 1 hit.
HAMAPiMF_00580. CH10. 1 hit.
InterProiIPR020818. Chaperonin_GroES.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]
PANTHERiPTHR10772. PTHR10772. 1 hit.
PfamiPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSiPR00297. CHAPERONIN10.
SMARTiSM00883. Cpn10. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
PROSITEiPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6F9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE
60 70 80 90
NGEVKPLDVK VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA
Length:97
Mass (Da):10,387
Last modified:March 29, 2005 - v1
Checksum:i76829E09B11217EF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti89S → N in CAA30738 (PubMed:2901493).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07850 Genomic DNA. Translation: CAA30697.1.
X07899 Genomic DNA. Translation: CAA30738.1.
U14003 Genomic DNA. Translation: AAA97041.1.
U00096 Genomic DNA. Translation: AAC77102.1.
AP009048 Genomic DNA. Translation: BAE78144.1.
PIRiS03931. BVECGS.
RefSeqiNP_418566.1. NC_000913.3.
WP_001026276.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77102; AAC77102; b4142.
BAE78144; BAE78144; BAE78144.
GeneIDi948655.
KEGGiecj:JW4102.
eco:b4142.
PATRICi32123853. VBIEscCol129921_4274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07850 Genomic DNA. Translation: CAA30697.1.
X07899 Genomic DNA. Translation: CAA30738.1.
U14003 Genomic DNA. Translation: AAA97041.1.
U00096 Genomic DNA. Translation: AAC77102.1.
AP009048 Genomic DNA. Translation: BAE78144.1.
PIRiS03931. BVECGS.
RefSeqiNP_418566.1. NC_000913.3.
WP_001026276.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AONX-ray3.00O/P/Q/R/S/T/U1-97[»]
1EGSNMR-A19-27[»]
1GRUelectron microscopy12.50O/P/Q/R/S/T/U1-97[»]
1PCQX-ray2.81O/P/Q/R/S/T/U1-97[»]
1PF9X-ray2.99O/P/Q/R/S/T/U1-97[»]
1SVTX-ray2.81O/P/Q/R/S/T/U1-97[»]
1SX4X-ray3.00O/P/Q/R/S/T/U1-97[»]
2C7Celectron microscopy7.70O/P/Q/R/S/T/U1-97[»]
2C7Delectron microscopy8.70O/P/Q/R/S/T/U1-97[»]
3WVLX-ray3.79O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b1-97[»]
3ZPZelectron microscopy8.90O/P/Q/R/S/T/U1-97[»]
3ZQ0electron microscopy9.20O/P/Q/R/S/T/U1-97[»]
3ZQ1electron microscopy15.90O/P/Q/R/S/T/U1-97[»]
ProteinModelPortaliP0A6F9.
SMRiP0A6F9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262198. 133 interactors.
DIPiDIP-9835N.
IntActiP0A6F9. 28 interactors.
MINTiMINT-5232475.
STRINGi511145.b4142.

2D gel databases

SWISS-2DPAGEP0A6F9.

Proteomic databases

EPDiP0A6F9.
PaxDbiP0A6F9.
PRIDEiP0A6F9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77102; AAC77102; b4142.
BAE78144; BAE78144; BAE78144.
GeneIDi948655.
KEGGiecj:JW4102.
eco:b4142.
PATRICi32123853. VBIEscCol129921_4274.

Organism-specific databases

EchoBASEiEB0595.
EcoGeneiEG10600. groS.

Phylogenomic databases

eggNOGiENOG4105K5Y. Bacteria.
COG0234. LUCA.
HOGENOMiHOG000133897.
InParanoidiP0A6F9.
KOiK04078.
OMAiVMGENEI.
PhylomeDBiP0A6F9.

Enzyme and pathway databases

BioCyciEcoCyc:EG10600-MONOMER.
ECOL316407:JW4102-MONOMER.
MetaCyc:EG10600-MONOMER.
SABIO-RKP0A6F9.

Miscellaneous databases

EvolutionaryTraceiP0A6F9.
PROiP0A6F9.

Family and domain databases

CDDicd00320. cpn10. 1 hit.
Gene3Di2.30.33.40. 1 hit.
HAMAPiMF_00580. CH10. 1 hit.
InterProiIPR020818. Chaperonin_GroES.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]
PANTHERiPTHR10772. PTHR10772. 1 hit.
PfamiPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSiPR00297. CHAPERONIN10.
SMARTiSM00883. Cpn10. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
PROSITEiPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCH10_ECOLI
AccessioniPrimary (citable) accession number: P0A6F9
Secondary accession number(s): P05380, Q2M6G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: November 2, 2016
This is version 117 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.