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P65762 (PPIA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable peptidyl-prolyl cis-trans isomerase A
Short name=PPIase A
EC=5.2.1.8
Alternative name(s):
Rotamase A
Gene names
Name:ppiA
Ordered Locus Names:Rv0009, MT0011
ORF Names:MTCY10H4.08
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length182 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activity

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

response to iron ion

Inferred from expression pattern. Source: MTBBASE

   Cellular componentcytosol

Inferred from direct assay. Source: MTBBASE

extracellular region

Inferred from direct assay. Source: MTBBASE

plasma membrane

Inferred from direct assay. Source: MTBBASE

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from direct assay. Source: MTBBASE

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 182182Probable peptidyl-prolyl cis-trans isomerase A
PRO_0000064209

Regions

Domain13 – 181169PPIase cyclophilin-type

Secondary structure

1 ................................ 182
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P65762 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: B3D83E7F9486BFCA

FASTA18219,239
        10         20         30         40         50         60 
MADCDSVTNS PLATATATLH TNRGDIKIAL FGNHAPKTVA NFVGLAQGTK DYSTQNASGG 

        70         80         90        100        110        120 
PSGPFYDGAV FHRVIQGFMI QGGDPTGTGR GGPGYKFADE FHPELQFDKP YLLAMANAGP 

       130        140        150        160        170        180 
GTNGSQFFIT VGKTPHLNRR HTIFGEVIDA ESQRVVEAIS KTATDGNDRP TDPVVIESIT 


IS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842572 Genomic DNA. Translation: CAB02430.1.
AE000516 Genomic DNA. Translation: AAK44233.1.
PIRG70698.
RefSeqNP_214523.1. NC_000962.2.
NP_334419.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W74X-ray2.60A/B2-182[»]
ProteinModelPortalP65762.
SMRP65762. Positions 12-182.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000003596; EBMYCP00000003596; EBMYCG00000003594.
EBMYCT00000070037; EBMYCP00000068096; EBMYCG00000070032.
GeneID887087.
922451.
GenomeReviewsGene locus MT0011 in contig AE000516_GR.
Gene locus Rv0009 in contig AL123456_GR.
KEGGmtc:MT0011.
mtu:Rv0009.
PATRIC18121752. VBIMycTub22151_0012.
TIGRMT0011.

Organism-specific databases

TubercuListRv0009.

Phylogenomic databases

GeneTreeEBGT00050000015125.
HOGENOMHBG610621.
OMAHQDVPRE.
PhylomeDBP65762.
ProtClustDBCLSK790189.

Enzyme and pathway databases

BRENDA5.2.1.8. 3445.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KOK03767.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPIA_MYCTU
AccessionPrimary (citable) accession number: P65762
Secondary accession number(s): P71578
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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