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Protein

10 kDa chaperonin

Gene

groS

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

GO - Molecular functioni

  • ATP binding Source: InterPro
  • chaperone binding Source: GO_Central
  • metal ion binding Source: MTBBASE
  • unfolded protein binding Source: GO_Central

GO - Biological processi

  • cellular response to heat Source: MTBBASE
  • chaperone mediated protein folding requiring cofactor Source: GO_Central
  • growth Source: MTBBASE
  • regulation of transcription, DNA-templated Source: MTBBASE
  • response to antibiotic Source: MTBBASE
  • response to heat Source: MTBBASE
  • response to unfolded protein Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-7695-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
10 kDa chaperonin
Alternative name(s):
10 kDa antigen1 Publication
BCG-A heat shock protein1 Publication
GroES protein
Protein Cpn10
Gene namesi
Name:groS
Synonyms:cpn10, groES, mopB
Ordered Locus Names:Rv3418c
ORF Names:MTCY78.11
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3418c.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • extracellular region Source: MTBBASE
  • GroEL-GroES complex Source: GO_Central
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Essential, it cannot be deleted.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001747882 – 10010 kDa chaperoninAdd BLAST99

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Cross-linki100Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP9WPE5.

Expressioni

Inductioni

Induced in response to heat shock (45 degrees Celsius), pH 4, pH 10, ethanol, H2O2, hyperosmolarity and starvation (PubMed:18227175).1 Publication

Interactioni

Subunit structurei

Heptamer of 7 subunits arranged in a domed ring (Ref. 10, PubMed:12837792). 2 rings join in their base to form a spherical cage-like structure; both heptamers and tetradecamers exist in solution (PubMed:12837792).2 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi83332.Rv3418c.

Structurei

Secondary structure

1100
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Beta strandi12 – 17Combined sources6
Beta strandi19 – 24Combined sources6
Turni25 – 27Combined sources3
Beta strandi37 – 46Combined sources10
Beta strandi53 – 56Combined sources4
Beta strandi68 – 72Combined sources5
Beta strandi77 – 81Combined sources5
Beta strandi84 – 90Combined sources7
Helixi91 – 93Combined sources3
Beta strandi94 – 99Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HX5X-ray3.50A/B/C/D/E/F/G2-100[»]
1P3HX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N2-100[»]
1P82NMR-A2-26[»]
1P83NMR-A2-26[»]
ProteinModelPortaliP9WPE5.
SMRiP9WPE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GroES chaperonin family.Curated

Phylogenomic databases

eggNOGiENOG4105K5Y. Bacteria.
COG0234. LUCA.
KOiK04078.
OMAiEHESCCH.
PhylomeDBiP9WPE5.

Family and domain databases

CDDicd00320. cpn10. 1 hit.
Gene3Di2.30.33.40. 1 hit.
HAMAPiMF_00580. CH10. 1 hit.
InterProiIPR020818. Chaperonin_GroES.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]
PANTHERiPTHR10772. PTHR10772. 1 hit.
PfamiPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSiPR00297. CHAPERONIN10.
SMARTiSM00883. Cpn10. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
PROSITEiPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WPE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVNIKPLE DKILVQANEA ETTTASGLVI PDTAKEKPQE GTVVAVGPGR
60 70 80 90 100
WDEDGEKRIP LDVAEGDTVI YSKYGGTEIK YNGEEYLILS ARDVLAVVSK
Length:100
Mass (Da):10,804
Last modified:April 16, 2014 - v1
Checksum:iDE448187A56103FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60350 Genomic DNA. Translation: CAA42908.1.
M25258 Genomic DNA. Translation: AAA25340.1.
X13739 Genomic DNA. Translation: CAA32003.1.
AL123456 Genomic DNA. Translation: CCP46240.1.
PIRiS01381. BVMYBA.
RefSeqiNP_217935.1. NC_000962.3.
WP_003418028.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP46240; CCP46240; Rv3418c.
GeneIDi887583.
KEGGimtu:Rv3418c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60350 Genomic DNA. Translation: CAA42908.1.
M25258 Genomic DNA. Translation: AAA25340.1.
X13739 Genomic DNA. Translation: CAA32003.1.
AL123456 Genomic DNA. Translation: CCP46240.1.
PIRiS01381. BVMYBA.
RefSeqiNP_217935.1. NC_000962.3.
WP_003418028.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HX5X-ray3.50A/B/C/D/E/F/G2-100[»]
1P3HX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N2-100[»]
1P82NMR-A2-26[»]
1P83NMR-A2-26[»]
ProteinModelPortaliP9WPE5.
SMRiP9WPE5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3418c.

Proteomic databases

PaxDbiP9WPE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46240; CCP46240; Rv3418c.
GeneIDi887583.
KEGGimtu:Rv3418c.

Organism-specific databases

TubercuListiRv3418c.

Phylogenomic databases

eggNOGiENOG4105K5Y. Bacteria.
COG0234. LUCA.
KOiK04078.
OMAiEHESCCH.
PhylomeDBiP9WPE5.

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-7695-MONOMER.

Family and domain databases

CDDicd00320. cpn10. 1 hit.
Gene3Di2.30.33.40. 1 hit.
HAMAPiMF_00580. CH10. 1 hit.
InterProiIPR020818. Chaperonin_GroES.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]
PANTHERiPTHR10772. PTHR10772. 1 hit.
PfamiPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSiPR00297. CHAPERONIN10.
SMARTiSM00883. Cpn10. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
PROSITEiPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCH10_MYCTU
AccessioniPrimary (citable) accession number: P9WPE5
Secondary accession number(s): L0TFJ8, P09621
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.