10 kDa chaperonin - Escherichia coli (strain K12)

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P0A6F9 (CH10_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
10 kDa chaperonin

Alternative name(s):
GroES protein
Protein Cpn10

Gene names

Name:	groS
Synonyms:	groES, mopB
Ordered Locus Names:	b4142, JW4102

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	97 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell 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 response to heat Inferred from expression pattern PubMed 8349564. Source: EcoliWiki virion assembly Inferred from mutant phenotype PubMed 7015340. Source: EcoliWiki
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro unfolded protein binding Inferred from mutant phenotype PubMed 2573517. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-369169,EBI-369169
groL	P0A6F5	15	EBI-369169,EBI-543750

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 97

10 kDa chaperonin HAMAP-Rule MF_00580

PRO_0000174746

Amino acid modifications

Modified residue

N6-succinyllysine Ref.12

Experimental info

Sequence conflict

S → N in CAA30738. Ref.2

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6F9 [UniParc].

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

10,387

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

        70         80         90 
VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA

« Hide

References

	« Hide 'large scale' referencesShow '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 277:1453-1474(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.

PIR

BVECGS. S03931.

RefSeq

NP_418566.1. NC_000913.2.
YP_492285.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A6F9.

SMR

P0A6F9. Positions 1-97.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9835N.

IntAct

P0A6F9. 22 interactions.

MINT

MINT-5232475.

STRING

511145.b4142.

PTM databases

PhosSite

P0809397.

2D gel databases

SWISS-2DPAGE

P0A6F9.

Proteomic databases

PaxDb

P0A6F9.

PRIDE

P0A6F9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77102; AAC77102; b4142.
BAE78144; BAE78144; BAE78144.

GeneID

12933204.
948655.

KEGG

ecj:Y75_p4029.
eco:b4142.

PATRIC

32123853. VBIEscCol129921_4274.

Organism-specific databases

EchoBASE

EB0595.

EcoGene

EG10600. groS.

Phylogenomic databases

eggNOG

COG0234.

HOGENOM

HOG000133897.

K04078.

OMA

GYGVKVE.

ProtClustDB

PRK00364.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10600-MONOMER.
ECOL316407:JW4102-MONOMER.

Gene expression databases

Genevestigator

P0A6F9.

Family and domain databases

Gene3D

2.30.33.40. 1 hit.

HAMAP

MF_00580. CH10.

InterPro

IPR020818. Chaperonin_Cpn10.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]

PANTHER

PTHR10772. PTHR10772. 1 hit.

Pfam

PF00166. Cpn10. 1 hit.
[Graphical view]

PRINTS

PR00297. CHAPERONIN10.

SMART

SM00883. Cpn10. 1 hit.
[Graphical view]

SUPFAM

SSF50129. GroES_like. 1 hit.

PROSITE

PS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6F9.

Entry information

Entry name

CH10_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents