Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0T9P8 (CH60_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60 kDa chaperonin
Alternative name(s):
GroEL protein
Protein Cpn60
Gene names
Name:groL
Synonyms:groEL
Ordered Locus Names:ECP_4387
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
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
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein 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

Chain1 – 54854860 kDa chaperonin HAMAP-Rule MF_00600
PRO_0000256910

Amino acid modifications

Modified residue1171N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0T9P8 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: A14A15010C983175

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 
DKAVAAAVEE LKTLSVPCSD 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

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000247 Genomic DNA. Translation: ABG72331.1.
RefSeqYP_672232.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0T9P8.
SMRQ0T9P8. Positions 2-525.
ModBaseSearch...

Protein-protein interaction databases

STRING362663.ECP_4387.

Proteomic databases

PRIDEQ0T9P8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG72331; ABG72331; ECP_4387.
GeneID4190456.
KEGGecp:ECP_4387.
PATRIC18199715. VBIEscCol77757_4437.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0459.
HOGENOMHOG000076290.
KOK04077.
OMAYNGVITV.
PhylomeDBQ0T9P8.
ProtClustDBPRK00013.

Enzyme and pathway databases

BioCycECOL362663:GIY5-4429-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_ECOL5
AccessionPrimary (citable) accession number: Q0T9P8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 19, 2006
Last modified: May 1, 2013
This is version 45 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents