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Gene: ppiA

General annotation | Coordinates | Sequence | Genome Browser | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography


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General annotation
Gene nameppiA
Rv numberRv0009
Synonym(s)cfp22
TypeCDS
FunctionPPIASES ACCELERATE THE FOLDING OF PROTEINS [CATALYTIC ACTIVITY: CIS-TRANS ISOMERIZATION OF PROLINE IMIDIC PEPTIDE BONDS IN OLIGOPEPTIDES].
ProductPROBABLE IRON-REGULATED PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A PPIA (PPIase A) (ROTAMASE A)
Evidenceexperimental
CommentsRv0009, (MTCY10H4.08), len: 182. Probable ppiA (alternate gene name: cfp22), iron-regulated peptidyl-prolyl cis-trans isomerase A , equivalent to NP_301138.1|NC_002677 putative peptidyl-prolyl cis-trans isomerase from Mycobacterium leprae (182 aa), FASTA score: (90.1% identity in 182 aa overlap). Also highly similar to others e.g. T36725 from Streptomyces coelicolor (177 aa); T43805 from Halobacterium salinarum (180 aa); NP_219383.1|NC_000919 from Treponema pallidum (215 aa); etc. BELONGS TO THE CYCLOPHILIN-TYPE PPIASE FAMILY. Alternative start codon has been suggested.
Molecular mass (Da)19239.3
Isoelectric point6.2287
Gene length (bp)549
Protein length182
Location (kb)12.468


Functional categoryinformation pathways


ProteomicsThe product of this CDS corresponds to spots 4_74, 4_10, 3_328 and 3_361 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany, spots 0009 also identified by the Statens Serum Institute (Denmark), and spot identified in the University of California (USA) (see citations below). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Identified in the cytosol of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Detected by 2-DE and MS in M. tuberculosis H37Rv purified from phagosomes of infected murine bone marrow macrophages but not in H37Rv broth-cultures (See Mattow et al., 2006). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007).
TranscriptomemRNA identified by DNA microarray analysis: possibly down-regulated by hrcA|Rv2374c (see Stewart et al., 2002), and down-regulated after 96h of starvation (see Betts et al., 2002). DNA microarrays indicate induction by iron and IdeR|Rv2711 in M. tuberculosis H37Rv (See Rodriguez et al., 2002).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003) mutants available at TARGET website
RegulonPredicted to be in the IdeR|Rv2711 regulon (See Prakash et al., 2005).


Coordinates
TypeStartEndOrientation
CDS1246813016+


Protein sequence in FASTA format
>M. tuberculosis H37Rv | ppiA
MADCDSVTNSPLATATATLHTNRGDIKIALFGNHAPKTVANFVGLAQGTKDYSTQNASGGPSGPFYDGAVFHRVIQGFMI
QGGDPTGTGRGGPGYKFADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGKTPHLNRRHTIFGEVIDAESQRVVEAIS
KTATDGNDRPTDPVVIESITIS
Blastp: results
TransMembrane prediction using Hidden Markov Models: tmhmm
Microbe Genome Browser
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
Protein Data Bank1W74
PFAMProtein Family Domains


3D Structure Viewer


Orthologs/Cross-references
CDC1551MT0011
Enzyme Classification5.2.1.8
Gene Ontologypeptidyl-prolyl cis-trans isomerase activity
cytoplasm
protein folding
MbovisMb0009
MlepraeML0011
MmarinumMMAR_0011
MsmegmatisMSMEG_0024
UniProtP65762


Interacting Drugs/Compounds
TDR TargetsRv0009


Expression Data
TBDBRv0009


Bibliography
Mollenkopf HJ, Jungblut PR, Raupach B, Mattow J, Lamer S, Zimny-Arndt U, Schaible UE, Kaufmann SH,
A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet
Electrophoresis (1999) 20(11):2172-80
Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K, Kaufmann SH,
Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens
Mol Microbiol (1999) 33(6):1103-17
Betts JC, Lukey PT, Robb LC, McAdam RA, Duncan K,
Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
Mol Microbiol (2002) 43 :717
Rodriguez GM, Voskuil MI, Gold B, Schoolnik GK, Smith I,
ideR, An essential gene in mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response.
Infect Immun (2002) 70(7):3371-81
Stewart GR, Wernisch L, Stabler R, Mangan JA, Hinds J, Laing KG, Young DB, Butcher PD,
Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays
Microbiology (2002) 148 (Pt 10):3129-3138
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X,
Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain.
Mol Cell Proteomics (2003) 2(12):1284-96
Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR, Kaufmann SH,
Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen.
Electrophoresis (2003) 24 (19-20):3405-20
Henriksson LM, Johansson P, Unge T, Mowbray SL,
X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis.
Eur J Biochem (2004) 271(20):4107-13
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Prakash P, Yellaboina S, Ranjan A, Hasnain SE,
Computational prediction and experimental verification of novel IdeR binding sites in the upstream sequences of Mycobacterium tuberculosis open reading frames.
Bioinformatics (2005) 21(10):2161-6
Mattow J, Siejak F, Hagens K, Becher D, Albrecht D, Krah A, Schmidt F, Jungblut PR, Kaufmann SH, Schaible UE,
Proteins unique to intraphagosomally grown Mycobacterium tuberculosis.
Proteomics (2006) 6(8):2485-94
Malen H, Berven FS, Fladmark KE, Wiker HG,
Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv.
Proteomics (2007) 7(10):1702-18
Weldingh K, Rosenkrands I, Jacobsen S, Rasmussen PB, Elhay MJ, Andersen P,
Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins
Infect Immun (1998) 66(8):3492-500
Wong DK, Lee BY, Horwitz MA, Gibson BW,
Identification of fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two -dimensional gel electrophoresis and mass spectrometry
Infect Immun (1999) 67(1):327-36