groS

Functionⁱ

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

GO - Molecular functionⁱ

ATP binding Source: InterPro
chaperone binding Source: GO_Central
identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 3017973
metal ion binding Source: GO_Central
unfolded protein binding Source: GO_Central

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell cycle Source: UniProtKB-KW
cell division Source: UniProtKB-KW
chaperone cofactor-dependent protein refolding
Source: EcoCyc
Inferred from direct assayⁱ
- 10532860
protein folding
Source: CACAO
Inferred from direct assayⁱ
- 2192863
response to heat
Source: EcoliWiki
Inferred from expression patternⁱ
- 8349564
response to unfolded protein Source: GO_Central
virion assembly
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 7015340

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chaperone
Biological process	Cell cycle, Cell division

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10600-MONOMER MetaCyc:EG10600-MONOMER
SABIO-RKⁱ	P0A6F9

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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10600 groS

EcoGeneⁱ

EG10600 groS

Subcellular locationⁱ

Cytoplasm
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.

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.

GO - Cellular componentⁱ

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000174746	1 – 97	10 kDa chaperoninAdd BLAST		97

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	34	N6-succinyllysine1 Publication		1

Proteomic databases

EPDⁱ	P0A6F9
PaxDbⁱ	P0A6F9
PRIDEⁱ	P0A6F9

2D gel databases

SWISS-2DPAGEⁱ	P0A6F9

SWISS-2DPAGEⁱ

P0A6F9

Interactionⁱ

Subunit structureⁱ

Heptamer of 7 subunits arranged in a ring.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-369169,EBI-369169
groL	P0A6F5	31	EBI-369169,EBI-543750

Show more details

GO - Molecular functionⁱ

chaperone binding Source: GO_Central
identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 3017973
unfolded protein binding Source: GO_Central

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4262198, 222 interactors
ComplexPortalⁱ	CPX-2113 GroEL-GroES complex
Database of interacting proteins More...DIPⁱ	DIP-9835N
IntActⁱ	P0A6F9, 41 interactors
Molecular INTeraction database More...MINTⁱ	P0A6F9
STRINGⁱ	316385.ECDH10B_4335

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	2 – 5	Combined sources	4
Beta strandⁱ	7 – 14	Combined sources	8
Turnⁱ	20 – 23	Combined sources	4
Beta strandⁱ	37 – 43	Combined sources	7
Beta strandⁱ	45 – 47	Combined sources	3
Beta strandⁱ	51 – 53	Combined sources	3
Beta strandⁱ	64 – 67	Combined sources	4
Beta strandⁱ	74 – 78	Combined sources	5
Beta strandⁱ	81 – 87	Combined sources	7
Helixⁱ	88 – 90	Combined sources	3
Beta strandⁱ	91 – 96	Combined sources	6

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	3WVL	X-ray	3.79	O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b	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	[»]
	5OPX	X-ray	3.64	1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z	1-97	[»]
ProteinModelPortalⁱ	P0A6F9
SMRⁱ	P0A6F9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A6F9

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the GroES chaperonin family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105K5Y Bacteria COG0234 LUCA
HOGENOMⁱ	HOG000133897
InParanoidⁱ	P0A6F9
KEGG Orthology (KO) More...KOⁱ	K04078
OMAⁱ	VMGENEI
PhylomeDBⁱ	P0A6F9

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00320 cpn10, 1 hit
Gene3Dⁱ	2.30.33.40, 1 hit
HAMAPⁱ	MF_00580 CH10, 1 hit
InterProⁱ	View protein in InterPro IPR020818 Chaperonin_GroES IPR037124 Chaperonin_GroES_sf IPR018369 Chaprnonin_Cpn10_CS IPR011032 GroES-like_sf
PANTHERⁱ	PTHR10772 PTHR10772, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00166 Cpn10, 1 hit
PRINTSⁱ	PR00297 CHAPERONIN10
SMARTⁱ	View protein in SMART SM00883 Cpn10, 1 hit
SUPFAMⁱ	SSF50129 SSF50129, 1 hit
PROSITEⁱ	View protein in PROSITE PS00681 CHAPERONINS_CPN10, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0A6F9-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE 
        60         70         80         90 
NGEVKPLDVK VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA

Length:97

Mass (Da):10,387

Last modified:March 29, 2005 - v1

Checksum:ⁱ76829E09B11217EF

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	89	S → N in CAA30738 (PubMed:2901493).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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	S03931 BVECGS
NCBI Reference Sequences More...RefSeqⁱ	NP_418566.1, NC_000913.3 WP_001026276.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC77102; AAC77102; b4142 BAE78144; BAE78144; BAE78144
GeneIDⁱ	948655
KEGGⁱ	ecj:JW4102 eco:b4142
PATRICⁱ	fig\|1411691.4.peg.2558

Protein	Similar proteins		Species	Score	Length
P0A6F9	10 kDa chaperonin		ECO24		97
10 kDa chaperonin		ECO27		97
10 kDa chaperonin		ECO45		97
10 kDa chaperonin		ECO55		97
10 kDa chaperonin		ECO57		97
+211

Protein	Similar proteins		Species	Score	Length
P0A6F9	10 kDa chaperonin		YEREN		97
10 kDa chaperonin		Rouxiella sp. ERMR1:05		106
10 kDa chaperonin		Rahnella sp. AA		106
UPI0009FEB1CE		Ewingella americana		117
10 kDa chaperonin		Serratia sp. Ag1		98
+458

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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	S03931 BVECGS
NCBI Reference Sequences More...RefSeqⁱ	NP_418566.1, NC_000913.3 WP_001026276.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	3WVL	X-ray	3.79	O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b	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	[»]
	5OPX	X-ray	3.64	1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z	1-97	[»]
ProteinModelPortalⁱ	P0A6F9
SMRⁱ	P0A6F9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262198, 222 interactors
ComplexPortalⁱ	CPX-2113 GroEL-GroES complex
Database of interacting proteins More...DIPⁱ	DIP-9835N
IntActⁱ	P0A6F9, 41 interactors
Molecular INTeraction database More...MINTⁱ	P0A6F9
STRINGⁱ	316385.ECDH10B_4335

2D gel databases

SWISS-2DPAGEⁱ	P0A6F9

SWISS-2DPAGEⁱ

P0A6F9

Proteomic databases

EPDⁱ	P0A6F9
PaxDbⁱ	P0A6F9
PRIDEⁱ	P0A6F9

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC77102; AAC77102; b4142 BAE78144; BAE78144; BAE78144
GeneIDⁱ	948655
KEGGⁱ	ecj:JW4102 eco:b4142
PATRICⁱ	fig\|1411691.4.peg.2558

Organism-specific databases

EchoBASEⁱ	EB0595
EcoGeneⁱ	EG10600 groS

Phylogenomic databases

eggNOGⁱ	ENOG4105K5Y Bacteria COG0234 LUCA
HOGENOMⁱ	HOG000133897
InParanoidⁱ	P0A6F9
KEGG Orthology (KO) More...KOⁱ	K04078
OMAⁱ	VMGENEI
PhylomeDBⁱ	P0A6F9

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10600-MONOMER MetaCyc:EG10600-MONOMER
SABIO-RKⁱ	P0A6F9

Miscellaneous databases

EvolutionaryTraceⁱ	P0A6F9
Protein Ontology More...PROⁱ	PR:P0A6F9

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00320 cpn10, 1 hit
Gene3Dⁱ	2.30.33.40, 1 hit
HAMAPⁱ	MF_00580 CH10, 1 hit
InterProⁱ	View protein in InterPro IPR020818 Chaperonin_GroES IPR037124 Chaperonin_GroES_sf IPR018369 Chaprnonin_Cpn10_CS IPR011032 GroES-like_sf
PANTHERⁱ	PTHR10772 PTHR10772, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00166 Cpn10, 1 hit
PRINTSⁱ	PR00297 CHAPERONIN10
SMARTⁱ	View protein in SMART SM00883 Cpn10, 1 hit
SUPFAMⁱ	SSF50129 SSF50129, 1 hit
PROSITEⁱ	View protein in PROSITE PS00681 CHAPERONINS_CPN10, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CH10_ECOLI
Accessionⁱ	P0A6F9Primary (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:	June 20, 2018
	This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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

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UniProtKB - P0A6F9 (CH10_ECOLI)

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10 kDa chaperonin

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

2D gel databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ