groS:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

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Standard name

GroES

Synonyms

Cpn10 chaperonin GroES, small subunit of GroESL[1], GroE[2][1], B4142[2][1], Hdh[2][1], TabA product[2][1], GroS[2][1], GroES[2][1], MopB[2][1] , ECK4136, groES, JW4102, mopB, TabB, b4142

Product description

GroES, chaperone binds to Hsp60 in pres. Mg-ATP, suppressing its ATPase activity[2][3];

Component of GroEL-GroES Chaperonin-CPLX[3]

Chaperonin Cpn10; GroESL small subunit GroES; phage morphogenesis[4]

EC number (for enzymes)


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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0042963

phage assembly

PMID:7015340[5]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0009408

response to heat

PMID:8349564[6]

IEP: Inferred from Expression Pattern

P

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of GroEL-GroES Chaperonin-CPLX

could be indirect

Protein

dnaK

PMID:15690043[7]

Experiment(s):EBI-885556, EBI-892166

Protein

dnaN

PMID:15690043[7]

Experiment(s):EBI-885556, EBI-892166

Protein

fusA

PMID:15690043[7]

Experiment(s):EBI-885556

Protein

htpG

PMID:15690043[7]

Experiment(s):EBI-885556

Protein

mreB

PMID:15690043[7]

Experiment(s):EBI-885556

Protein

hldD

PMID:15690043[7]

Experiment(s):EBI-885556, EBI-892166

Protein

tig

PMID:15690043[7]

Experiment(s):EBI-885556, EBI-892166

Protein

minD

PMID:16606699[8]

Experiment(s):EBI-1147540

Protein

nrdI

PMID:16606699[8]

Experiment(s):EBI-1147540

Protein

rplO

PMID:16606699[8]

Experiment(s):EBI-1147540

Protein

sufE

PMID:16606699[8]

Experiment(s):EBI-1147540

Protein

rpmI

PMID:16606699[8]

Experiment(s):EBI-1147540

Protein

nadE

PMID:16606699[8]

Experiment(s):EBI-1147540

Protein

rpsB

PMID:15690043[7]

Experiment(s):EBI-892166

Protein

slyD

PMID:15690043[7]

Experiment(s):EBI-892166

Protein

ybbP

PMID:15690043[7]

Experiment(s):EBI-892166

Protein

fepB

PMID:15690043[7]

Experiment(s):EBI-892166

Protein

grpE

PMID:19402753[9]

LCMS(ID Probability):99.0 MALDI(Z-score):25.437584

Protein

clpA

PMID:19402753[9]

MALDI(Z-score):27.054664

Protein

dnaN

PMID:19402753[9]

LCMS(ID Probability):99.6 MALDI(Z-score):39.136060

Protein

rfaD

PMID:19402753[9]

LCMS(ID Probability):99.6 MALDI(Z-score):39.802389

Protein

tig

PMID:19402753[9]

LCMS(ID Probability):99.6 MALDI(Z-score):39.990229

Protein

lon

PMID:19402753[9]

MALDI(Z-score):22.459071

Protein

clpB

PMID:19402753[9]

MALDI(Z-score):28.355102

Protein

ybbP

PMID:19402753[9]

LCMS(ID Probability):99.6

Protein

ybbN

PMID:19402753[9]

MALDI(Z-score):36.591327

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK
VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA
Length

97

Mol. Wt

10.386 kDa

pI

4.9 (calculated)

Extinction coefficient

1,490 (calc based on 1 Y, 0 W, and 0 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Modification Site

71

phosphorylation site at Y71

probability greater than 75%

PMID:17938405[10]

Domain

2..95

PF00166 Chaperonin 10 Kd subunit

PMID:19920124[11]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=groS taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16131967

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:948655

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0013566

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0A6F9

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10600

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10600

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:948655

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000593

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0595

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ Tilly, K et al. (1981) Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc. Natl. Acad. Sci. U.S.A. 78 1629-33 PubMed
  6. ↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed
  7. ↑ 7.00 7.01 7.02 7.03 7.04 7.05 7.06 7.07 7.08 7.09 7.10 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  8. ↑ 8.0 8.1 8.2 8.3 8.4 8.5 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  9. ↑ 9.0 9.1 9.2 9.3 9.4 9.5 9.6 9.7 9.8 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  10. ↑ Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed
  11. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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