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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

BURPS1710b_A0907

Organism
Burkholderia pseudomallei (strain 1710b)
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 bindingi51 – 511CalciumCombined sources
Metal bindingi52 – 521Calcium; via carbonyl oxygenCombined sources
Metal bindingi112 – 1121CalciumCombined sources
Metal bindingi113 – 1131Calcium; via amide nitrogen and carbonyl oxygenCombined sources

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. 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

CalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BioCyciBPSE320372:GBYB-4705-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomeraseUniRule annotation (EC:5.2.1.8UniRule annotation)
Gene namesi
Ordered Locus Names:BURPS1710b_A0907Imported
OrganismiBurkholderia pseudomallei (strain 1710b)Imported
Taxonomic identifieri320372 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000002700: Chromosome II

Interactioni

Protein-protein interaction databases

STRINGi320372.BURPS1710b_A0907.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2SNMR-A1-113[»]
3UF8X-ray1.50A2-113[»]
3UQBX-ray1.90A2-113[»]
3VAWX-ray1.55A4-113[»]
4DZ2X-ray2.00A/B2-113[»]
4DZ3X-ray2.00A/B2-113[»]
4FN2X-ray1.95A/B2-113[»]
4G50X-ray1.75A/B2-113[»]
4GGQX-ray1.95A/B/C/D2-113[»]
4GIVX-ray2.45A/B2-113[»]
ProteinModelPortaliQ3JK38.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3JK38.

Family & Domainsi

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000154887.
KOiK01802.
OMAiPFEFPIG.
OrthoDBiEOG6DRPKW.

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.

Q3JK38-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVVTTESGL KYEDLTEGSG AEARAGQTVS VHYTGWLTDG QKFDSSKDRN
60 70 80 90 100
DPFAFVLGGG MVIKGWDEGV QGMKVGGVRR LTIPPQLGYG ARGAGGVIPP
110
NATLVFEVEL LDV
Length:113
Mass (Da):11,930
Last modified:November 8, 2005 - v1
Checksum:i10AB26FB56F3F284
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000125 Genomic DNA. Translation: ABA51599.1.
RefSeqiYP_336065.1. NC_007435.1.

Genome annotation databases

EnsemblBacteriaiABA51599; ABA51599; BURPS1710b_A0907.
GeneIDi3694107.
KEGGibpm:BURPS1710b_A0907.
PATRICi19242233. VBIBurPse115837_4954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000125 Genomic DNA. Translation: ABA51599.1.
RefSeqiYP_336065.1. NC_007435.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2SNMR-A1-113[»]
3UF8X-ray1.50A2-113[»]
3UQBX-ray1.90A2-113[»]
3VAWX-ray1.55A4-113[»]
4DZ2X-ray2.00A/B2-113[»]
4DZ3X-ray2.00A/B2-113[»]
4FN2X-ray1.95A/B2-113[»]
4G50X-ray1.75A/B2-113[»]
4GGQX-ray1.95A/B/C/D2-113[»]
4GIVX-ray2.45A/B2-113[»]
ProteinModelPortaliQ3JK38.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi320372.BURPS1710b_A0907.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA51599; ABA51599; BURPS1710b_A0907.
GeneIDi3694107.
KEGGibpm:BURPS1710b_A0907.
PATRICi19242233. VBIBurPse115837_4954.

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000154887.
KOiK01802.
OMAiPFEFPIG.
OrthoDBiEOG6DRPKW.

Enzyme and pathway databases

BioCyciBPSE320372:GBYB-4705-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ3JK38.

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. Woods D.E., Nierman W.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1710bImported.
  2. "Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with 1-{[(4-methylphenyl)thio]acetyl}piperidine."
    Seattle Structural Genomics Center for Infectious Disease (SSGCID)
    Zheng S., Barnwal R., Leeper T., Varani G.
    Submitted (AUG-2010) to the PDB data bank
    Cited for: STRUCTURE BY NMR.
  3. "A structural biology approach enables the development of antimicrobials targeting bacterial immunophilins."
    Begley D.W., Fox D., Jenner D., Juli C., Pierce P.G., Abendroth J., Muruthi M., Safford K., Anderson V., Atkins K., Barnes S.R., Moen S.O., Raymond A.C., Stacy R., Myler P.J., Staker B.L., Harmer N.J., Norville I.H.
    , Holzgrabe U., Sarkar-Tyson M., Edwards T.E., Lorimer D.D.
    Antimicrob. Agents Chemother. 58:1458-1467(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-113 IN COMPLEX WITH CALCIUM.

Entry informationi

Entry nameiQ3JK38_BURP1
AccessioniPrimary (citable) accession number: Q3JK38
Entry historyi
Integrated into UniProtKB/TrEMBL: November 8, 2005
Last sequence update: November 8, 2005
Last modified: February 4, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete 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.