P0A6F9 (CH10_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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)

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 MF_00580
Subunit structure	Heptamer of 7 subunits arranged in a ring.
Subcellular location	Cytoplasm HAMAP MF_00580.
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 phage assembly Inferred from mutant phenotype. Source: EcoliWiki protein folding Inferred from electronic annotation. Source: InterPro response to heat Inferred from expression pattern. Source: EcoliWiki
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro identical protein binding Inferred from physical interaction. Source: IntAct unfolded protein binding Inferred from mutant phenotype. 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

97

10 kDa chaperonin HAMAP MF_00580

PRO_0000174746

Experimental info

Sequence conflict

89

1

S → N in CAA30738. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

97

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

9 – 14

6

Turn

20 – 23

4

Beta strand

37 – 43

7

Beta strand

64 – 67

4

Beta strand

74 – 80

7

Beta strand

82 – 87

6

Turn

88 – 90

3

Beta strand

91 – 95

5

Sequences

	Sequence		Length	Mass (Da)
	P0A6F9 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: 76829E09B11217EF	FASTA	97	10,387
	10 20 30 40 50 60 MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK 70 80 90 VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA

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: 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

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.

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. 23 interactions.

MINT

MINT-5232475.

PTM databases

PhosSite

P0A6F9.

2D gel databases

SWISS-2DPAGE

P0A6F9.

ECO2DBASE

C015.4. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000723; EBESCP00000000723; EBESCG00000000600.
EBESCT00000015352; EBESCP00000014643; EBESCG00000014412.

GeneID

948655.

GenomeReviews

Gene locus JW4102 in contig AP009048_GR.
Gene locus b4142 in contig U00096_GR.

KEGG

ecj:JW4102.
eco:b4142.

PATRIC

32123853. VBIEscCol129921_4274.

Organism-specific databases

EchoBASE

EB0595.

EcoGene

EG10600. groS.

Phylogenomic databases

eggNOG

COG0234.

GeneTree

EBGT00050000009807.

HOGENOM

HBG703377.

OMA

YGVKVEK.

PhylomeDB

P0A6F9.

ProtClustDB

PRK00364.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10600-MONOMER.

Gene expression databases

Genevestigator

P0A6F9.

Family and domain databases

HAMAP

MF_00580. CH10.
[Tree]

InterPro

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

Gene3D

G3DSA:2.30.33.40. Chaprnin_Cpn10. 1 hit.

KO

K04078.

PANTHER

PTHR10772. Chaprnin_Cpn10. 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...

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:	January 25, 2012
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program