ppiA
- Type
- protein_coding
- Name
- ppiA
- Locus Name
-
Rv0009
- Product
-
Probable iron-regulated peptidyl-prolyl cis-trans isomerase A PpiA (PPIase A) (rotamase A)
- Functional Category
-
Information pathways
- Location
- 12468..13016 (+ strand)
- Gene Length
- 548 bp
- Nucleotides
-
TGGCAGACTGTGATTCCGTGACTAACAGCCCCCTTGCGACCGCTACCGCCACGCTGCACACTAACCGCGGCGACATCAAGATCGCCCTGTTCGGAAACCATGCGCCCAAGACCGTCGCCAATTTTGTGGGCCTTGCGCAGGGCACCAAGGACTATTCGACCCAAAACGCATCAGGTGGCCCGTCCGGCCCGTTCTACGACGGCGCGGTCTTTCACCGGGTGATCCAGGGCTTCATGATCCAGGGTGGCGATCCAACCGGGACGGGTCGCGGCGGACCCGGCTACAAGTTCGCCGACGAGTTCCACCCCGAGCTGCAATTCGACAAGCCCTATCTGCTCGCGATGGCCAACGCCGGTCCGGGCACCAACGGCTCACAGTTTTTCATCACCGTCGGCAAGACTCCGCACCTGAACCGGCGCCACACCATTTTCGGTGAAGTGATCGACGCGGAGTCACAGCGGGTTGTGGAGGCGATCTCCAAGACGGCCACCGACGGCAACGATCGGCCGACGGACCCGGTGGTGATCGAGTCGATCACCATCTCCTGA
- Drug Resistance
- Mutations
- Function
- PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000269|PubMed:15479239, ECO:0000269|PubMed:17141764}.
- Family
-
Cyclophilin-type PPIase family
- GO
-
- response to iron ion GO:0010039 biological_process
- peptidyl-prolyl cis-trans isomerase activity GO:0003755 molecular_function
- cell wall GO:0005618 cellular_component
- extracellular region GO:0005576 cellular_component
- cytosol GO:0005829 cellular_component
- plasma membrane GO:0005886 cellular_component
- protein folding GO:0006457 biological_process
- InterPro
1W74
- Name
- Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin) (Rotamase A)
- Family
- Cyclophilin-type PPIase family
- Protein Sequence
-
MADCDSVTNSPLATATATLHTNRGDIKIALFGNHAPKTVANFVGLAQGTKDYSTQNASGGPSGPFYDGAVFHRVIQGFMIQGGDPTGTGRGGPGYKFADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGKTPHLNRRHTIFGEVIDAESQRVVEAISKTATDGNDRPTDPVVIESITIS
- Mass
- 19,239 Da
- Length
- 182 Aa
Summary
Rv0009 doesn't seem to be a targeted by any drug.
Rv0009 doesn't seem to be involved in any pathway.
- X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis.
- Eur J Biochem. 2004 Oct;271(20):4107-13. doi: 10.1111/j.1432-1033.2004.04348.x.
- Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
- Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
- Cyclosporin A binding to Mycobacterium tuberculosis peptidyl-prolyl cis-trans isomerase A--investigation by CD, FTIR and fluorescence spectroscopy.
- FEBS Lett. 2006 Dec 22;580(30):6846-60. doi: 10.1016/j.febslet.2006.11.042. Epub 2006 Nov 27.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.