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UniProtKB - P0A6F5 (CH60_ECOLI)

Entry version 165 (25 May 2022)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

Chaperonin GroEL

Gene

groEL

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 its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed:2897629, PubMed:2573517, PubMed:10532860, PubMed:1676490, PubMed:8104102, PubMed:9285593, 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).

Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex (PubMed:9285593, PubMed:9285585, PubMed:19915138, PubMed:22445172).

Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation (PubMed:8861908, PubMed:9285585, PubMed:16684774, PubMed:22445172).

To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability (PubMed:9285593).

Finally, binding of ATP to the opposite trans ring of GroEL results in disassembly of the cis-ternary complex, which opens the cage and allows release of the folded protein (PubMed:9285593, PubMed:9285585).

Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form (PubMed:7915201, PubMed:7867798).

Can rescue kinetically trapped intermediates (PubMed:20603018).

GroEL shows ATPase activity (PubMed:379350, PubMed:1676490, PubMed:9285593).

ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding (PubMed:9285593).

19 Publications

Also plays a role in coupling between replication of the F plasmid and cell division of the cell.

1 Publication

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

2 Publications

Caution

Was originally designated as the ams protein.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

During the substrate-folding cycle, the two GroEL rings separate for effective substrate binding and chaperonin activity. Ring separation is triggered by ATP binding to the trans ring of the asymmetric GroEL:GroES complex and avoids formation of functionally impaired symmetric GroEL:GroES2 complexes (PubMed:29336887). Activity of the GroEL-GroES chaperonin complex requires Mg-ATP (PubMed:10532860, PubMed:9285593).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei51ATPUniRule annotationCombined sources2 Publications1 Publication1
Binding sitei415ATP; via amide nitrogenUniRule annotationCombined sources2 Publications1 Publication1
Binding sitei495ATPUniRule annotationCombined sources2 Publications1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi30 – 33ATPUniRule annotationCombined sources2 Publications1 Publication4
Nucleotide bindingi87 – 91ATPUniRule annotationCombined sources2 Publications1 Publication5
Nucleotide bindingi479 – 481ATPUniRule annotationCombined sources2 Publications1 Publication3

<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, Isomerase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10599-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		5.6.1.7, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0A6F5

<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:
Chaperonin GroELUniRule annotationCurated (EC:5.6.1.7UniRule annotation2 Publications)
Alternative name(s):
60 kDa chaperoninUniRule annotation
Chaperonin-601 PublicationUniRule annotation
Short name:
Cpn601 PublicationUniRule annotation
GroEL proteinCurated
<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:groEL1 PublicationUniRule annotation
Synonyms:groLUniRule annotation, mopA
Ordered Locus Names:b4143, JW4103
<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2A → S: Complex stability is significantly decreased; when associated with S-76, same residues as in M.tuberculosis. 1 Publication1
Mutagenesisi76E → S: Complex stability is significantly decreased; when associated with S-2, same residues as in M.tuberculosis. 1 Publication1
Mutagenesisi109A → C: Forms inter-ring disulfide bonds. Prevents ring separation and leads to the formation of high amounts of symmetric GroEL:GroES2 complexes. 1 Publication1
Mutagenesisi398D → A: Can bind ATP with normal affinity, but is defective in ATPase activity. Binds non-native rhodanese, but cannot release the protein. 1 Publication1
Mutagenesisi461E → K: Temperature-sensitive lethal mutant. At nonpermissive temperature, the rate of general translation is reduced and a defined group of cytoplasmic proteins are translated but fail to reach native form. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4296299

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<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_00000633582 – 548Chaperonin GroELAdd BLAST547

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
Modified residuei51N6-succinyllysine1 Publication1
Modified residuei117N6-acetyllysine; alternate1 Publication1
Modified residuei117N6-succinyllysine; alternate1 Publication1
Modified residuei277N6-succinyllysine1 Publication1
Modified residuei321N6-succinyllysine1 Publication1
Modified residuei390N6-succinyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated reversibly during heat shock.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A6F5

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

More...PaxDbi		P0A6F5

PRoteomics IDEntifications database

More...PRIDEi		P0A6F5

2D gel databases

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

More...SWISS-2DPAGEi		P0A6F5

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P0A6F5

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0A6F5

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P0A6F5

<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

Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back (PubMed:1361169, PubMed:15327959, PubMed:7935790, PubMed:8846220, PubMed:9285585).

Interacts with the co-chaperonin GroES (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).

11 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		4263077, 558 interactors
852957, 7 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-339N

Protein interaction database and analysis system

More...IntActi		P0A6F5, 700 interactors

Molecular INTeraction database

More...MINTi		P0A6F5

STRING: functional protein association networks

More...STRINGi		511145.b4143

<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

1548
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P0A6F5

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

More...SMRi		P0A6F5

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		P0A6F5

<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 general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Each subunit is composed of an apical domain that binds non-folded proteins and GroES, an intermediate domain and an equatorial domain that binds ATP and is involved in inter-ring interactions (PubMed:7935790, PubMed:16288915). Forms a large central channel that appears to traverse the entire length of the cylinder with no obstruction (PubMed:7935790). The central channel of GroEL functions as two cavities, one in each ring, that are separated from each other by the crystallographically disordered 23-amino-acid C-terminal segments of the seven subunits (PubMed:9285585). The entry and exit of polypeptide seem to be restricted to the apical end of each ring (PubMed:9285585).3 Publications
Modulating the volume of the GroEL central cavity affects folding speed in accordance with confinement theory. Small proteins fold more rapidly as the size of the cage is gradually reduced to a point where restriction in space slows folding dramatically. For larger proteins, either expanding or reducing cage volume decelerate folding (PubMed:16751100). A stepwise reduction in cage size results in a gradual loss of cell viability (PubMed:18418386).2 Publications

<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 chaperonin (HSP60) family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0459, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_016503_3_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A6F5

Identification of Orthologs from Complete Genome Data

More...OMAi		TDTDKME

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A6F5

Family and domain databases

Conserved Domains Database

More...CDDi		cd03344, GroEL, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.560.10, 1 hit
3.30.260.10, 1 hit
3.50.7.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00600, CH60, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR018370, Chaperonin_Cpn60_CS
IPR001844, Cpn60/GroEL
IPR002423, Cpn60/GroEL/TCP-1
IPR027409, GroEL-like_apical_dom_sf
IPR027413, GROEL-like_equatorial_sf
IPR027410, TCP-1-like_intermed_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00118, Cpn60_TCP1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00298, CHAPERONIN60

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48592, SSF48592, 1 hit
SSF52029, SSF52029, 1 hit
SSF54849, SSF54849, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02348, GroEL, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00296, CHAPERONINS_CPN60, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6F5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT 
        60         70         80         90        100
KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII 
       110        120        130        140        150
TEGLKAVAAG MNPMDLKRGI DKAVTAAVEE LKALSVPCSD SKAIAQVGTI 
       160        170        180        190        200
SANSDETVGK LIAEAMDKVG KEGVITVEDG TGLQDELDVV EGMQFDRGYL 
       210        220        230        240        250
SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV AKAGKPLLII 
       260        270        280        290        300
AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 
       310        320        330        340        350
ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR 
       360        370        380        390        400
QQIEEATSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL 
       410        420        430        440        450
HATRAAVEEG VVAGGGVALI RVASKLADLR GQNEDQNVGI KVALRAMEAP 
       460        470        480        490        500
LRQIVLNCGE EPSVVANTVK GGDGNYGYNA ATEEYGNMID MGILDPTKVT 
       510        520        530        540 
RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM
Length:548
Mass (Da):57,329
Last modified:January 23, 2007 - v2
<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:iCD3A0FB505F74AD1
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA23934 differs from that shown. Reason: Frameshift.Curated

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 conflicti83 – 86DAAG → GALQ in CAA30739 (PubMed:2901493).Curated4
Sequence conflicti262L → A in CAA30698 (PubMed:2897629).Curated1
Sequence conflicti267M → I in CAA30698 (PubMed:2897629).Curated1
Sequence conflicti343Q → R in AAA23934 (PubMed:2578448).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: CAA30698.1
U14003 Genomic DNA Translation: AAA97042.1
U00096 Genomic DNA Translation: AAC77103.1
AP009048 Genomic DNA Translation: BAE78145.1
X07899 Genomic DNA Translation: CAA30739.1
M11294 Genomic DNA Translation: AAA23934.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...PIRi		S56371, BVECGL

NCBI Reference Sequences

More...RefSeqi		NP_418567.1, NC_000913.3
WP_000729117.1, NZ_STEB01000014.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC77103; AAC77103; b4143
BAE78145; BAE78145; BAE78145

Database of genes from NCBI RefSeq genomes

More...GeneIDi		66671945
948665

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW4103
eco:b4143

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2557

<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: CAA30698.1
U14003 Genomic DNA Translation: AAA97042.1
U00096 Genomic DNA Translation: AAC77103.1
AP009048 Genomic DNA Translation: BAE78145.1
X07899 Genomic DNA Translation: CAA30739.1
M11294 Genomic DNA Translation: AAA23934.1 Frameshift.
PIRiS56371, BVECGL
RefSeqiNP_418567.1, NC_000913.3
WP_000729117.1, 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-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1DK7X-ray2.02A/B191-336[»]
1DKDX-ray2.10A/B/C/D191-336[»]
1FY9X-ray2.20A191-376[»]
1FYAX-ray2.20A191-376[»]
1GR5electron microscopy7.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1GRLX-ray2.80A/B/C/D/E/F/G1-548[»]
1GRUelectron microscopy12.50A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1JONX-ray2.50A191-345[»]
1KIDX-ray1.70A188-376[»]
1KP8X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1LA1X-ray2.06A188-379[»]
1MNFX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1OELX-ray2.80A/B/C/D/E/F/G2-548[»]
1PCQX-ray2.81A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1PF9X-ray2.99A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1SS8X-ray2.70A/B/C/D/E/F/G2-525[»]
1SVTX-ray2.81A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1SX3X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-526[»]
1SX4X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1XCKX-ray2.92A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Celectron microscopy7.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Delectron microscopy8.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Eelectron microscopy9.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2CGTelectron microscopy8.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2EU1X-ray3.29A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
2NWCX-ray3.02A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2YEYX-ray3.30A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
3C9Velectron microscopy4.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3CAUelectron microscopy4.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3VZ6X-ray1.50A191-376[»]
3VZ7X-ray1.80A191-376[»]
3VZ8X-ray1.90A/B/C191-376[»]
3WVLX-ray3.79A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
3ZPZelectron microscopy8.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3ZQ0electron microscopy9.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
3ZQ1electron microscopy15.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
4AAQelectron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AARelectron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AASelectron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AAUelectron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AB2electron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AB3electron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4V43X-ray3.521/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z2-548[»]
4WGLX-ray3.13A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4WSCX-ray3.04A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
5OPWX-ray3.19A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
5OPXX-ray3.64A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
5W0Selectron microscopy3.50A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
7PBJelectron microscopy3.40Ad/Ae/Ak/Al/Ar/As/Ay/Az/Bf/Bg/Bm/Bn/Bt/Bu2-525[»]
7PBXelectron microscopy3.43Ac/Ad/Ai/Aj/Ao/Ap/Au/Av/Ba/Bb/Bg/Bh/Bm/Bn2-525[»]
7VWXelectron microscopy7.60A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
AlphaFoldDBiP0A6F5
SMRiP0A6F5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263077, 558 interactors
852957, 7 interactors
ComplexPortaliCPX-2113, GroEL-GroES complex
DIPiDIP-339N
IntActiP0A6F5, 700 interactors
MINTiP0A6F5
STRINGi511145.b4143

Chemistry databases

ChEMBLiCHEMBL4296299

PTM databases

CarbonylDBiP0A6F5
iPTMnetiP0A6F5
MetOSiteiP0A6F5

2D gel databases

SWISS-2DPAGEiP0A6F5

Proteomic databases

jPOSTiP0A6F5
PaxDbiP0A6F5
PRIDEiP0A6F5

Genome annotation databases

EnsemblBacteriaiAAC77103; AAC77103; b4143
BAE78145; BAE78145; BAE78145
GeneIDi66671945
948665
KEGGiecj:JW4103
eco:b4143
PATRICifig|1411691.4.peg.2557

Organism-specific databases

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

More...EchoBASEi		EB0594

Phylogenomic databases

eggNOGiCOG0459, Bacteria
HOGENOMiCLU_016503_3_0_6
InParanoidiP0A6F5
OMAiTDTDKME
PhylomeDBiP0A6F5

Enzyme and pathway databases

BioCyciEcoCyc:EG10599-MONOMER
BRENDAi5.6.1.7, 2026
SABIO-RKiP0A6F5

Miscellaneous databases

EvolutionaryTraceiP0A6F5

Protein Ontology

More...PROi		PR:P0A6F5

Family and domain databases

CDDicd03344, GroEL, 1 hit
Gene3Di1.10.560.10, 1 hit
3.30.260.10, 1 hit
3.50.7.10, 1 hit
HAMAPiMF_00600, CH60, 1 hit
InterProiView protein in InterPro
IPR018370, Chaperonin_Cpn60_CS
IPR001844, Cpn60/GroEL
IPR002423, Cpn60/GroEL/TCP-1
IPR027409, GroEL-like_apical_dom_sf
IPR027413, GROEL-like_equatorial_sf
IPR027410, TCP-1-like_intermed_sf
PfamiView protein in Pfam
PF00118, Cpn60_TCP1, 1 hit
PRINTSiPR00298, CHAPERONIN60
SUPFAMiSSF48592, SSF48592, 1 hit
SSF52029, SSF52029, 1 hit
SSF54849, SSF54849, 1 hit
TIGRFAMsiTIGR02348, GroEL, 1 hit
PROSITEiView protein in PROSITE
PS00296, CHAPERONINS_CPN60, 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 nameiCH60_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: P0A6F5
Secondary accession number(s): P06139, Q2M6G1
<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: January 1, 1988
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 165 of the entry and version 2 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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