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P65762 (PPIA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase A
Short name=PPIase A
EC=5.2.1.8
Alternative name(s):
Cyclophilin
Rotamase A
Gene names
Name:ppiA
Ordered Locus Names:Rv0009, MT0011
ORF Names:MTCY10H4.08
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
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. Ref.3 Ref.4

Catalytic activity

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

Subunit structure

Homodimer. Ref.4

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 182182Peptidyl-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

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Cyclosporin A binding to Mycobacterium tuberculosis peptidyl-prolyl cis-trans isomerase A--investigation by CD, FTIR and fluorescence spectroscopy."
Mitra D., Mukherjee S., Das A.K.
FEBS Lett. 580:6846-6860(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis."
Henriksson L.M., Johansson P., Unge T., Mowbray S.L.
Eur. J. Biochem. 271:4107-4113(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-182, FUNCTION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842572 Genomic DNA. Translation: CAB02430.1.
AE000516 Genomic DNA. Translation: AAK44233.1.
AL123456 Genomic DNA. Translation: CCP42731.1.
PIRG70698.
RefSeqNP_214523.1. NC_000962.3.
NP_334419.1. NC_002755.2.
YP_006513323.1. NC_018143.1.

3D structure databases

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

Protein-protein interaction databases

STRING83332.Rv0009.

Proteomic databases

PaxDbP65762.
PRIDEP65762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK44233; AAK44233; MT0011.
GeneID13315986.
887087.
922451.
KEGGmtc:MT0011.
mtu:Rv0009.
mtv:RVBD_0009.
PATRIC18121752. VBIMycTub22151_0012.

Organism-specific databases

TubercuListRv0009.

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
KOK03767.
OMADDLTHDG.
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]
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...

Other

EvolutionaryTraceP65762.

Entry information

Entry namePPIA_MYCTU
AccessionPrimary (citable) accession number: P65762
Secondary accession number(s): L0T5F1, P71578
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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