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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

  1. ATP binding Source: InterPro
  2. identical protein binding Source: IntAct
  3. unfolded protein binding Source: EcoCyc

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. protein folding Source: UniProtKB-HAMAP
  4. response to heat Source: EcoliWiki
  5. 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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: 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

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 979710 kDa chaperoninPRO_0000174746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341N6-succinyllysine1 Publication

Proteomic databases

PaxDbiP0A6F9.
PRIDEiP0A6F9.

2D gel databases

SWISS-2DPAGEP0A6F9.

PTM databases

PhosSiteiP0809397.

Expressioni

Gene expression databases

GenevestigatoriP0A6F9.

Interactioni

Subunit structurei

Heptamer of 7 subunits arranged in a ring.

Binary interactionsi

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

Protein-protein interaction databases

DIPiDIP-9835N.
IntActiP0A6F9. 28 interactions.
MINTiMINT-5232475.
STRINGi511145.b4142.

Structurei

Secondary structure

1
97
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi7 – 148Combined sources
Turni20 – 234Combined sources
Beta strandi37 – 437Combined sources
Beta strandi45 – 473Combined sources
Beta strandi51 – 533Combined sources
Beta strandi64 – 674Combined sources
Beta strandi74 – 785Combined sources
Beta strandi81 – 877Combined sources
Helixi88 – 903Combined sources
Beta strandi91 – 966Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-97.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6F9.

Family & Domainsi

Sequence similaritiesi

Belongs to the GroES chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0234.
HOGENOMiHOG000133897.
InParanoidiP0A6F9.
KOiK04078.
OMAiGYGVKVE.
OrthoDBiEOG6GFGSD.
PhylomeDBiP0A6F9.

Family and domain databases

Gene3Di2.30.33.40. 1 hit.
HAMAPiMF_00580. CH10.
InterProiIPR020818. Chaperonin_Cpn10.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891S → N in CAA30738. (PubMed:2901493)Curated

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.
YP_492285.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77102; AAC77102; b4142.
BAE78144; BAE78144; BAE78144.
GeneIDi12933204.
948655.
KEGGiecj:Y75_p4029.
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.
YP_492285.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9835N.
IntActiP0A6F9. 28 interactions.
MINTiMINT-5232475.
STRINGi511145.b4142.

PTM databases

PhosSiteiP0809397.

2D gel databases

SWISS-2DPAGEP0A6F9.

Proteomic databases

PaxDbiP0A6F9.
PRIDEiP0A6F9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77102; AAC77102; b4142.
BAE78144; BAE78144; BAE78144.
GeneIDi12933204.
948655.
KEGGiecj:Y75_p4029.
eco:b4142.
PATRICi32123853. VBIEscCol129921_4274.

Organism-specific databases

EchoBASEiEB0595.
EcoGeneiEG10600. groS.

Phylogenomic databases

eggNOGiCOG0234.
HOGENOMiHOG000133897.
InParanoidiP0A6F9.
KOiK04078.
OMAiGYGVKVE.
OrthoDBiEOG6GFGSD.
PhylomeDBiP0A6F9.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A6F9.
PROiP0A6F9.

Gene expression databases

GenevestigatoriP0A6F9.

Family and domain databases

Gene3Di2.30.33.40. 1 hit.
HAMAPiMF_00580. CH10.
InterProiIPR020818. Chaperonin_Cpn10.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Homologous plant and bacterial proteins chaperone oligomeric protein assembly."
    Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T., Georgopoulos C., Hendrix R.W., Ellis R.J.
    Nature 333:330-334(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Control of cell division by sex factor F in Escherichia coli. III. Participation of the groES (mopB) gene of the host bacteria."
    Miki T., Orita T., Furuno M., Horiuchi T.
    J. Mol. Biol. 201:327-338(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES."
    Martin J., Geromanos S., Tempst P., Hartl F.U.
    Nature 366:279-282(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-74.
  7. "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases."
    Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C.
    Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-18.
  8. Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  10. Cited for: PROTEIN SEQUENCE OF 1-4.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  11. "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.
  12. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-34.
    Strain: K12.
  13. "Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli."
    Li G., Young K.D.
    Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  14. "The crystal structure of the GroES co-chaperonin at 2.8-A resolution."
    Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., Deisenhofer J.
    Nature 379:37-45(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  15. "The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex."
    Xu Z., Horwich A.L., Sigler P.B.
    Nature 388:741-750(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  16. Cited for: STRUCTURE BY NMR OF 19-27.

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: January 7, 2015
This is version 101 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

External Data

Dasty 3

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 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.