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UniProtKB - P0A6F9 (CH10_ECOLI)

Entry version 150 (23 Feb 2022)
Sequence version 1 (29 Mar 2005)
Previous versions | rss
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Protein

Co-chaperonin GroES

Gene

groES

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Together with the chaperonin GroEL, plays an essential role in assisting protein folding (PubMed:2897629, PubMed:2573517, PubMed:10532860, PubMed:1676490, PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391).

The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391).

GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel (PubMed:9285585).

Regulates the ATPase activity of GroEL (PubMed:1676490, PubMed:1361169).

11 Publications

(Microbial infection) Essential for the assembly of several bacteriophages.

2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity of the GroEL-GroES chaperonin complex requires Mg-ATP.1 Publication

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10600-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0A6F9

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Co-chaperonin GroESUniRule annotationCurated
Alternative name(s):
10 kDa chaperoninUniRule annotationCurated
Chaperonin-101 PublicationUniRule annotation
Short name:
Cpn101 PublicationUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:groES1 PublicationUniRule annotation
Synonyms:groS, mopB
Ordered Locus Names:b4142, JW4102
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<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

Keywords - Cellular componenti

Cytoplasm

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001747461 – 97Co-chaperonin GroESAdd BLAST97

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei34N6-succinyllysine1 Publication1

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A6F9

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P0A6F9

PRoteomics IDEntifications database

More...PRIDEi		P0A6F9

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0A6F9

<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>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heptamer of 7 subunits arranged in a ring (PubMed:1361169, PubMed:9285585).

Interacts with the chaperonin GroEL (PubMed:1361169, PubMed:7638600, PubMed:7638601, PubMed:8618836, PubMed:8663256, PubMed:9285585, PubMed:25174333). Can form asymmetrical complexes, composed of one GroEL and one GroES, and symmetrical complexes, formed between one GroEL and two GroES oligomers (PubMed:1361169, PubMed:7638600, PubMed:7638601, PubMed:8618836, PubMed:8663256, PubMed:25174333). The asymmetrical complex is the functional unit (PubMed:7638600, PubMed:7638601, PubMed:25912285). It was suggested that the symmetric heterooligomer may represent a transient intermediate in the chaperonin protein folding cycle (PubMed:8618836, PubMed:8663256). Another study shows that the symmetric heterooligomers are substantially populated only in the presence of proteins that cannot be folded by the chaperonin (PubMed:25912285).

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4262198, 222 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2113, GroEL-GroES complex

Database of interacting proteins

More...DIPi		DIP-9835N

Protein interaction database and analysis system

More...IntActi		P0A6F9, 41 interactors

Molecular INTeraction database

More...MINTi		P0A6F9

STRING: functional protein association networks

More...STRINGi		511145.b4142

<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

197
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0A6F9

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A6F9

<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

Belongs to the GroES chaperonin family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0234, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_132825_1_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A6F9

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A6F9

Family and domain databases

Conserved Domains Database

More...CDDi		cd00320, cpn10, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.33.40, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00580, CH10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR020818, Chaperonin_GroES
IPR037124, Chaperonin_GroES_sf
IPR018369, Chaprnonin_Cpn10_CS
IPR011032, GroES-like_sf

The PANTHER Classification System

More...PANTHERi		PTHR10772, PTHR10772, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00166, Cpn10, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00297, CHAPERONIN10

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00883, Cpn10, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50129, SSF50129, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00681, CHAPERONINS_CPN10, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0A6F9-1 [UniParc]FASTAAdd 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i76829E09B11217EF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti89S → N in CAA30738 (PubMed:2901493).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		S03931, BVECGS

NCBI Reference Sequences

More...RefSeqi		NP_418566.1, NC_000913.3
WP_001026276.1, NZ_STEB01000014.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC77102; AAC77102; b4142
BAE78144; BAE78144; BAE78144

Database of genes from NCBI RefSeq genomes

More...GeneIDi		67414760
948655

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW4102
eco:b4142

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2558

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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
PIRiS03931, BVECGS
RefSeqiNP_418566.1, NC_000913.3
WP_001026276.1, NZ_STEB01000014.1

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 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[»]
3WVLX-ray3.79O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b1-97[»]
3ZPZelectron microscopy8.90O/P/Q/R/S/T/U1-97[»]
3ZQ0electron microscopy9.20O/P/Q/R/S/T/U1-97[»]
3ZQ1electron microscopy15.90O/P/Q/R/S/T/U1-97[»]
5OPXX-ray3.641/2/O/P/Q/R/S/T/U/V/W/X/Y/Z1-97[»]
SMRiP0A6F9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262198, 222 interactors
ComplexPortaliCPX-2113, GroEL-GroES complex
DIPiDIP-9835N
IntActiP0A6F9, 41 interactors
MINTiP0A6F9
STRINGi511145.b4142

2D gel databases

SWISS-2DPAGEiP0A6F9

Proteomic databases

jPOSTiP0A6F9
PaxDbiP0A6F9
PRIDEiP0A6F9

Genome annotation databases

EnsemblBacteriaiAAC77102; AAC77102; b4142
BAE78144; BAE78144; BAE78144
GeneIDi67414760
948655
KEGGiecj:JW4102
eco:b4142
PATRICifig|1411691.4.peg.2558

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0595

Phylogenomic databases

eggNOGiCOG0234, Bacteria
HOGENOMiCLU_132825_1_1_6
InParanoidiP0A6F9
PhylomeDBiP0A6F9

Enzyme and pathway databases

BioCyciEcoCyc:EG10600-MONOMER
SABIO-RKiP0A6F9

Miscellaneous databases

EvolutionaryTraceiP0A6F9

Protein Ontology

More...PROi		PR:P0A6F9

Family and domain databases

CDDicd00320, cpn10, 1 hit
Gene3Di2.30.33.40, 1 hit
HAMAPiMF_00580, CH10, 1 hit
InterProiView protein in InterPro
IPR020818, Chaperonin_GroES
IPR037124, Chaperonin_GroES_sf
IPR018369, Chaprnonin_Cpn10_CS
IPR011032, GroES-like_sf
PANTHERiPTHR10772, PTHR10772, 1 hit
PfamiView protein in Pfam
PF00166, Cpn10, 1 hit
PRINTSiPR00297, CHAPERONIN10
SMARTiView protein in SMART
SM00883, Cpn10, 1 hit
SUPFAMiSSF50129, SSF50129, 1 hit
PROSITEiView protein in PROSITE
PS00681, CHAPERONINS_CPN10, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCH10_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A6F9
Secondary accession number(s): P05380, Q2M6G2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: February 23, 2022
This is version 150 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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