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Protein

60 kDa chaperonin

Gene

groL

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa chaperonin
Alternative name(s):
GroEL protein
Heat shock protein 60
Protein Cpn60
Gene namesi
Name:groL
Synonyms:cpnL, groEL, hsp60, mopA
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›145›14560 kDa chaperoninPRO_0000063583Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi262724.TTC1714.

Structurei

Secondary structure

1
145
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi11 – 133Combined sources
Turni17 – 204Combined sources
Beta strandi21 – 3616Combined sources
Helixi39 – 5012Combined sources
Beta strandi56 – 638Combined sources
Helixi65 – 7612Combined sources
Beta strandi82 – 865Combined sources
Helixi91 – 10515Combined sources
Turni112 – 1154Combined sources
Helixi118 – 1203Combined sources
Helixi123 – 1253Combined sources
Beta strandi127 – 1348Combined sources
Beta strandi139 – 1446Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SRVX-ray1.70A1-145[»]
ProteinModelPortaliP61491.
SMRiP61491. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61491.

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Phylogenomic databases

eggNOGiENOG4105CJ9. Bacteria.
COG0459. LUCA.

Family and domain databases

Gene3Di3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.

Sequencei

Sequence statusi: Fragment.

P61491-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GYQFDKGYIS PYFVTNPETM EAVLEDAFIL IVEKKVSNVR ELLPILEQVA
60 70 80 90 100
QTGKPLLIIA EDVEGEALAT LVVNKLRGTL SVAAVKAPGF GDRRKEMLKD
110 120 130 140
IAAVTGGTVI SEELGFKLEN ATLSMLGRAE RVRITKDETT IVGGK
Length:145
Mass (Da):15,736
Last modified:May 24, 2005 - v2
Checksum:i7E02F2AE0DF7C024
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei145 – 1451

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SRVX-ray1.70A1-145[»]
ProteinModelPortaliP61491.
SMRiP61491. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC1714.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CJ9. Bacteria.
COG0459. LUCA.

Miscellaneous databases

EvolutionaryTraceiP61491.

Family and domain databases

Gene3Di3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCH60_THETH
AccessioniPrimary (citable) accession number: P61491
Secondary accession number(s): P45746, Q60018, Q9RA44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2005
Last modified: December 9, 2015
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1SRV.Curated

Keywords - Technical termi

3D-structure

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.