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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

TTHA0346

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi5 – 51Zinc 1Combined sources
Metal bindingi6 – 61Zinc 1Combined sources
Metal bindingi33 – 331Zinc 1; via tele nitrogenCombined sources
Binding sitei62 – 621Succinate; via carbonyl oxygenCombined sources
Metal bindingi145 – 1451Zinc 2; via pros nitrogenCombined sources
Metal bindingi147 – 1471Zinc 2; via tele nitrogenCombined sources
Metal bindingi149 – 1491Zinc 2; via tele nitrogenCombined sources

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, RotamaseUniRule annotation

Keywords - Ligandi

Metal-bindingCombined sources, ZincCombined sources

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-363-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomeraseUniRule annotation (EC:5.2.1.8UniRule annotation)
Gene namesi
Ordered Locus Names:TTHA0346Imported
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)Imported
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0346.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CGMX-ray2.41A1-149[»]
3CGNX-ray2.70A1-149[»]
3LUOX-ray2.55A1-149[»]
4ODKX-ray1.40A1-149[»]
4ODLX-ray2.92A/B1-149[»]
4ODMX-ray1.75A/B/C/D1-149[»]
4ODNX-ray1.60A1-149[»]
4ODOX-ray1.60A/B/C1-149[»]
4ODPX-ray1.75A1-64[»]
A126-149[»]
4ODQX-ray2.00A1-64[»]
A126-149[»]
4ODRX-ray1.93A/B1-64[»]
A/B126-149[»]
ProteinModelPortaliQ5SLE7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLE7.

Family & Domainsi

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG1047.
HOGENOMiHOG000154889.
KOiK03775.
OMAiHMLAGQT.
OrthoDBiEOG6Q8J79.
PhylomeDBiQ5SLE7.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SLE7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVGQDKVVT IRYTLQVEGE VLDQGELSYL HGHRNLIPGL EEALEGREEG
60 70 80 90 100
EAFQAHVPAE KAYGPHDPEG VQVVPLSAFP EDAEVVPGAQ FYAQDMEGNP
110 120 130 140
MPLTVVAVEG EEVTVDFNHP LAGKDLDFQV EVVKVREATP EELLHGHAH
Length:149
Mass (Da):16,313
Last modified:December 20, 2004 - v1
Checksum:iFE9ABD7980C37C76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70169.1.
RefSeqiYP_143612.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70169; BAD70169; BAD70169.
GeneIDi3168679.
KEGGittj:TTHA0346.
PATRICi23955654. VBITheThe93045_0346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70169.1.
RefSeqiYP_143612.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CGMX-ray2.41A1-149[»]
3CGNX-ray2.70A1-149[»]
3LUOX-ray2.55A1-149[»]
4ODKX-ray1.40A1-149[»]
4ODLX-ray2.92A/B1-149[»]
4ODMX-ray1.75A/B/C/D1-149[»]
4ODNX-ray1.60A1-149[»]
4ODOX-ray1.60A/B/C1-149[»]
4ODPX-ray1.75A1-64[»]
A126-149[»]
4ODQX-ray2.00A1-64[»]
A126-149[»]
4ODRX-ray1.93A/B1-64[»]
A/B126-149[»]
ProteinModelPortaliQ5SLE7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0346.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70169; BAD70169; BAD70169.
GeneIDi3168679.
KEGGittj:TTHA0346.
PATRICi23955654. VBITheThe93045_0346.

Phylogenomic databases

eggNOGiCOG1047.
HOGENOMiHOG000154889.
KOiK03775.
OMAiHMLAGQT.
OrthoDBiEOG6Q8J79.
PhylomeDBiQ5SLE7.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-363-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SLE7.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579Imported.
  2. "Crystal structure determination and functional characterization of the metallochaperone SlyD from Thermus thermophilus."
    Low C., Neumann P., Tidow H., Weininger U., Haupt C., Friedrich-Epler B., Scholz C., Stubbs M.T., Balbach J.
    J. Mol. Biol. 398:375-390(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH SUCCINATE AND ZINC.
  3. "Structure of SlyD delta-IF from Thermus thermophilus in complex with FK506."
    Quistgaard E.M., Low C., Nordlund P.
    Submitted (DEC-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-64 AND 126-149 IN COMPLEX WITH ZINC.
  4. "Structure of SlyD delta-IF from Thermus thermophilus in complex with S2-W23A peptide."
    Quistgaard E.M., Low C., Nordlund P.
    Submitted (DEC-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-64 AND 126-149.
  5. "Structure of SlyD delta-IF from Thermus thermophilus in complex with S3 peptide."
    Quistgaard E.M., Low C., Nordlund P.
    Submitted (DEC-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-64 AND 126-149.
  6. "Structure of SlyD from Thermus thermophilus in complex with FK506."
    Quistgaard E.M., Low C., Nordlund P.
    Submitted (DEC-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
  7. "Structure of SlyD from Thermus thermophilus in complex with S2 peptide."
    Quistgaard E.M., Low C., Nordlund P.
    Submitted (DEC-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS).
  8. "Structure of SlyD from Thermus thermophilus in complex with S2-plus peptide."
    Quistgaard E.M., Low C., Nordlund P.
    Submitted (DEC-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
  9. "Structure of SlyD from Thermus thermophilus in complex with S2-W23A peptide."
    Quistgaard E.M., Low C., Nordlund P.
    Submitted (DEC-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
  10. "Structure of SlyD from Thermus thermophilus in complex with T1 peptide."
    Quistgaard E.M., Low C., Nordlund P.
    Submitted (DEC-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS).

Entry informationi

Entry nameiQ5SLE7_THET8
AccessioniPrimary (citable) accession number: Q5SLE7
Entry historyi
Integrated into UniProtKB/TrEMBL: December 20, 2004
Last sequence update: December 20, 2004
Last modified: March 31, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.