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P0A6F7 (CH60_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
60 kDa chaperonin
Alternative name(s):
GroEL protein
Protein Cpn60
Gene names
Name:groL
Synonyms:groEL, mopA
Ordered Locus Names:Z5748, ECs5124
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions By similarity. HAMAP-Rule MF_00600

Subunit structure

Oligomer of 14 subunits composed of two stacked rings of 7 subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

protein refolding

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 54854760 kDa chaperonin HAMAP-Rule MF_00600
PRO_0000063360

Amino acid modifications

Modified residue1171N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A6F7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CD3A0FB505F74AD1

FASTA54857,329
        10         20         30         40         50         60 
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI 

        70         80         90        100        110        120 
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI 

       130        140        150        160        170        180 
DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG 

       190        200        210        220        230        240 
TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV 

       250        260        270        280        290        300 
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 

       310        320        330        340        350        360 
ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY 

       370        380        390        400        410        420 
DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI 

       430        440        450        460        470        480 
RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA 

       490        500        510        520        530        540 
ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG 


MGGMGGMM

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG59342.1.
BA000007 Genomic DNA. Translation: BAB38547.1.
PIRD91269.
RefSeqNP_290776.1. NC_002655.2.
NP_313151.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A6F7.
SMRP0A6F7. Positions 2-525.
ModBaseSearch...

Protein-protein interaction databases

IntActP0A6F7. 1 interaction.
MINTMINT-1299311.
STRING155864.Z5748.

Proteomic databases

PRIDEP0A6F7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG59342; AAG59342; Z5748.
BAB38547; BAB38547; BAB38547.
GeneID913705.
959980.
KEGGece:Z5748.
ecs:ECs5124.
PATRIC18359865. VBIEscCol44059_5068.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0459.
HOGENOMHOG000076290.
KOK04077.
OMAYNGVITV.
ProtClustDBPRK00013.

Enzyme and pathway databases

BioCycECOL386585:GJFA-5130-MONOMER.

Family and domain databases

HAMAPMF_00600. CH60.
InterProIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
[Graphical view]
PANTHERPTHR11353. PTHR11353. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00298. CHAPERONIN60.
SUPFAMSSF48592. GroEL-ATPase. 1 hit.
TIGRFAMsTIGR02348. GroEL. 1 hit.
PROSITEPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCH60_ECO57
AccessionPrimary (citable) accession number: P0A6F7
Secondary accession number(s): P06139
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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