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P0A6F9

- CH10_ECOLI

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Protein
10 kDa chaperonin
Gene
groS, groES, mopB, b4142, JW4102

Gene:

groS, groES, mopB, b4142, JW4102
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

UniProt

P0A6F9 - CH10_ECOLI

Protein:

10 kDa chaperonin
Protein Existence: Experimental evidence at protein level

Functioni

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

GO - Molecular functioni

  1. ATP bindingInferred from electronic annotationi Source: InterPro
  2. identical protein bindingInferred from physical interactioni PubMed 10077571PubMed 16858726 Source: IntAct
  3. unfolded protein bindingInferred from mutant phenotypei PubMed 2573517 Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. ATP bindingInferred from electronic annotationi Source: InterPro
  2. identical protein bindingInferred from physical interactioni PubMed 10077571PubMed 16858726 Source: IntAct
  3. unfolded protein bindingInferred from mutant phenotypei PubMed 2573517 Source: EcoCyc
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-RKiP0A6F9.

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
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.1 Publication

GO - Cellular componenti

  1. cytosolInferred from direct assayi PubMed 16858726 Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Chaini1 – 979710 kDa chaperoninUniRule annotation
PRO_0000174746

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Modified residuei341N6-succinyllysine1 Publication

Proteomic databases

PaxDbiP0A6F9.
PRIDEiP0A6F9.

2D gel databases

SWISS-2DPAGEiP0A6F9.

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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.

Miscellaneous databases

EvolutionaryTraceiP0A6F9.

Family & Domainsi

Sequence similaritiesi

Belongs to the GroES chaperonin family.

Phylogenomic databases

eggNOGiCOG0234.
HOGENOMiHOG000133897.
KOiK04078.
OMAiGYGVKVE.
OrthoDBiEOG6GFGSD.
PhylomeDBiP0A6F9.
ProtClustDBiPRK00364.

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]FASTA

« Hide

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti891S → N in CAA30738. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRiBVECGS. S03931.
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:
EMBL
GenBank
DDBJ
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 .
PIRi BVECGS. S03931.
RefSeqi NP_418566.1. NC_000913.3.
YP_492285.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AON X-ray 3.00 O/P/Q/R/S/T/U 1-97 [» ]
1EGS NMR - A 19-27 [» ]
1GRU electron microscopy 12.50 O/P/Q/R/S/T/U 1-97 [» ]
1PCQ X-ray 2.81 O/P/Q/R/S/T/U 1-97 [» ]
1PF9 X-ray 2.99 O/P/Q/R/S/T/U 1-97 [» ]
1SVT X-ray 2.81 O/P/Q/R/S/T/U 1-97 [» ]
1SX4 X-ray 3.00 O/P/Q/R/S/T/U 1-97 [» ]
2C7C electron microscopy 7.70 O/P/Q/R/S/T/U 1-97 [» ]
2C7D electron microscopy 8.70 O/P/Q/R/S/T/U 1-97 [» ]
3ZPZ electron microscopy 8.90 O/P/Q/R/S/T/U 1-97 [» ]
3ZQ0 electron microscopy 9.20 O/P/Q/R/S/T/U 1-97 [» ]
3ZQ1 electron microscopy 15.90 O/P/Q/R/S/T/U 1-97 [» ]
ProteinModelPortali P0A6F9.
SMRi P0A6F9. Positions 1-97.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-9835N.
IntActi P0A6F9. 28 interactions.
MINTi MINT-5232475.
STRINGi 511145.b4142.

PTM databases

PhosSitei P0809397.

2D gel databases

SWISS-2DPAGEi P0A6F9.

Proteomic databases

PaxDbi P0A6F9.
PRIDEi P0A6F9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77102 ; AAC77102 ; b4142 .
BAE78144 ; BAE78144 ; BAE78144 .
GeneIDi 12933204.
948655.
KEGGi ecj:Y75_p4029.
eco:b4142.
PATRICi 32123853. VBIEscCol129921_4274.

Organism-specific databases

EchoBASEi EB0595.
EcoGenei EG10600. groS.

Phylogenomic databases

eggNOGi COG0234.
HOGENOMi HOG000133897.
KOi K04078.
OMAi GYGVKVE.
OrthoDBi EOG6GFGSD.
PhylomeDBi P0A6F9.
ProtClustDBi PRK00364.

Enzyme and pathway databases

BioCyci EcoCyc:EG10600-MONOMER.
ECOL316407:JW4102-MONOMER.
SABIO-RKi P0A6F9.

Miscellaneous databases

EvolutionaryTracei P0A6F9.
PROi P0A6F9.

Gene expression databases

Genevestigatori P0A6F9.

Family and domain databases

Gene3Di 2.30.33.40. 1 hit.
HAMAPi MF_00580. CH10.
InterProi IPR020818. Chaperonin_Cpn10.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view ]
PANTHERi PTHR10772. PTHR10772. 1 hit.
Pfami PF00166. Cpn10. 1 hit.
[Graphical view ]
PRINTSi PR00297. CHAPERONIN10.
SMARTi SM00883. Cpn10. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 1 hit.
PROSITEi PS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  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.

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: April 16, 2014
This is version 95 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

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