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P0A6F9 (CH10_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
10 kDa chaperonin
Alternative name(s):
GroES protein
Protein Cpn10
Gene names
Name:groS
Synonyms:groES, mopB
Ordered Locus Names:b4142, JW4102
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length97 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. HAMAP-Rule MF_00580

Subunit structure

Heptamer of 7 subunits arranged in a ring.

Subcellular location

Cytoplasm. 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. Ref.13

Sequence similarities

Belongs to the GroES chaperonin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-369169,EBI-369169
groLP0A6F525EBI-369169,EBI-543750

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 979710 kDa chaperonin HAMAP-Rule MF_00580
PRO_0000174746

Amino acid modifications

Modified residue341N6-succinyllysine Ref.12

Experimental info

Sequence conflict891S → N in CAA30738. Ref.2

Secondary structure

..................... 97
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6F9 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: 76829E09B11217EF

FASTA9710,387
        10         20         30         40         50         60 
MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK 

        70         80         90 
VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.
Submitted (SEP-1994) to UniProtKB
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]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
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]"Interplay of structure and disorder in cochaperonin mobile loops."
Landry S.J., Taher A., Georgopoulos C., van der Vies S.M.
Proc. Natl. Acad. Sci. U.S.A. 93:11622-11627(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 19-27.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRBVECGS. S03931.
RefSeqNP_418566.1. NC_000913.3.
YP_492285.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortalP0A6F9.
SMRP0A6F9. Positions 1-97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9835N.
IntActP0A6F9. 28 interactions.
MINTMINT-5232475.
STRING511145.b4142.

PTM databases

PhosSiteP0809397.

2D gel databases

SWISS-2DPAGEP0A6F9.

Proteomic databases

PaxDbP0A6F9.
PRIDEP0A6F9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77102; AAC77102; b4142.
BAE78144; BAE78144; BAE78144.
GeneID12933204.
948655.
KEGGecj:Y75_p4029.
eco:b4142.
PATRIC32123853. VBIEscCol129921_4274.

Organism-specific databases

EchoBASEEB0595.
EcoGeneEG10600. groS.

Phylogenomic databases

eggNOGCOG0234.
HOGENOMHOG000133897.
KOK04078.
OMAGYGVKVE.
OrthoDBEOG6GFGSD.
PhylomeDBP0A6F9.
ProtClustDBPRK00364.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0A6F9.

Family and domain databases

Gene3D2.30.33.40. 1 hit.
HAMAPMF_00580. CH10.
InterProIPR020818. Chaperonin_Cpn10.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]
PANTHERPTHR10772. PTHR10772. 1 hit.
PfamPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSPR00297. CHAPERONIN10.
SMARTSM00883. Cpn10. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
PROSITEPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6F9.
PROP0A6F9.

Entry information

Entry nameCH10_ECOLI
AccessionPrimary (citable) accession number: P0A6F9
Secondary accession number(s): P05380, Q2M6G2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene