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Reviewed, UniProtKB/Swiss-Prot P0A6F9 (CH10_ECOLI)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length97 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 MF_00580

Subunit structure

Heptamer of 7 subunits arranged in a ring. HAMAP MF_00580

Subcellular location

Cytoplasm. HAMAP MF_00580

Sequence similarities

Belongs to the groES chaperonin family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasm
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

protein folding

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytosol

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 979710 kDa chaperonin HAMAP MF_00580
PRO_0000174746

Experimental info

Sequence conflict891S → N in CAA30738. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6F9-1 [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: 2897629] [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: 2901493] [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: 7610040] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 7901771] [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: 8506346] [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: 9298646] [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: 9600841] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-4.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[11]"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: 8538739] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[12]"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: 9285585] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[13]"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: 8876186] [Abstract]
Cited for: STRUCTURE BY NMR OF 19-27.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
RefSeqAP_004643.1.
NP_418566.1.

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9835N.
IntActP0A6F9. 24 interactions.

PTM databases

PhosSiteP0A6F9.

2-D gel databases

SWISS-2DPAGEP0A6F9.
ECO2DBASEC015.4. 6TH EDITION.

Genome annotation databases

GeneID948655.
GenomeReviewsGene locus JW4102 in contig AP009048_GR.
Gene locus b4142 in contig U00096_GR.
KEGGecj:JW4102.
eco:b4142.

Organism-specific databases

EchoBASEEB0595.
EcoGeneEG10600. groS.
CMRSearch...

Phylogenomic databases

HOGENOMP0A6F9.
OMAP0A6F9. SEKIDGE.

Enzyme and pathway databases

BioCycEcoCyc:EG10600-MON.

Family and domain databases

HAMAPMF_00580.
[Tree]
InterProIPR001476. Chaprnonin_Cpn10.
IPR018369. Chaprnonin_Cpn10_CS.
[Graphical view]
Gene3DG3DSA:2.30.33.40. Chaprnin_Cpn10. 1 hit.
PANTHERPTHR10772. Chaprnin_Cpn10. 1 hit.
PfamPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSPR00297. CHAPERONIN10.
ProDomPD000566. Chaprnin_Cpn10. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents