pstP
- Type
- protein_coding
- Name
- pstP
- Locus Name
-
Rv0018c
- Product
-
Phosphoserine/threonine phosphatase PstP
- Functional Category
-
Regulatory proteins
- Location
- 21637..23181 (- strand)
- Gene Length
- 1544 bp
- Nucleotides
-
GTGGCGCGCGTGACCCTGGTCCTGCGATACGCGGCGCGCAGCGATCGCGGCTTGGTACGCGCCAACAACGAAGACTCGGTCTACGCTGGGGCACGGCTATTGGCCCTGGCCGACGGCATGGGTGGGCATGCGGCCGGCGAGGTGGCGTCCCAGTTGGTGATTGCCGCATTGGCCCATCTCGATGACGACGAGCCCGGTGGCGATCTGCTGGCCAAGCTGGATGCCGCGGTGCGCGCCGGCAACTCGGCTATCGCAGCGCAAGTCGAGATGGAGCCCGATCTCGAAGGCATGGGTACCACGCTCACCGCAATCCTGTTCGCGGGCAACCGGCTCGGCCTGGTGCATATCGGTGACTCGCGCGGTTACCTGCTGCGCGACGGTGAGCTGACGCAGATCACCAAGGACGACACGTTTGTCCAAACGCTGGTCGACGAAGGCCGGATCACCCCGGAGGAGGCGCACAGCCACCCGCAACGCTCGTTGATCATGCGGGCGTTGACCGGCCATGAGGTCGAACCGACGCTGACCATGCGAGAAGCCCGCGCCGGTGATCGTTACCTGCTGTGCTCGGACGGGTTGTCCGATCCGGTTAGCGATGAAACTATCCTCGAGGCCCTGCAGATCCCCGAGGTTGCCGAGAGCGCTCACCGCCTCATTGAACTGGCGCTGCGCGGCGGCGGCCCCGACAACGTCACTGTCGTCGTCGCCGACGTCGTCGACTACGACTACGGCCAGACCCAACCGATTCTGGCCGGGGCGGTCTCAGGCGACGACGACCAACTGACCCTGCCCAACACCGCCGCCGGCCGGGCCTCTGCCATCAGCCAGCGCAAGGAGATCGTTAAACGCGTTCCGCCACAGGCCGATACATTCAGTCGGCCACGGTGGTCGGGCCGACGGCTAGCATTCGTTGTCGCACTGGTGACCGTGCTGATGACTGCGGGCCTGCTCATTGGTCGCGCGATCATCCGCAGCAACTACTACGTAGCGGACTACGCCGGCAGCGTGTCCATCATGCGGGGGATTCAAGGGTCGCTACTGGGCATGTCCCTGCACCAGCCTTACCTGATGGGCTGCCTCAGCCCGCGTAACGAGCTGTCGCAGATCAGCTACGGACAGTCTGGGGGCCCTCTCGACTGCCATCTGATGAAACTGGAGGATCTGCGACCGCCGGAGCGCGCACAGGTTCGGGCCGGTCTCCCGGCCGGCACTCTCGATGACGCCATCGGGCAGTTGCGCGAACTGGCGGCCAACTCCCTGCTGCCGCCTTGCCCGGCGCCGCGTGCCACGTCCCCGCCCGGGCGCCCGGCCCCACCCACCACCAGCGAGACAACCGAACCAAACGTCACCTCCTCGCCAGCCTCTCCATCACCCACCACCTCCGCGCCGGCCCCCACCGGAACTACTCCTGCCATCCCCACGAGTGCCTCCCCGGCAGCGCCCGCGTCGCCGCCGACGCCTTGGCCCGTCACCAGCTCGCCGACGATGGCCGCACTTCCGCCACCCCCGCCTCAGCCGGGCATCGACTGCCGGGCGGCGGCATG
- Drug Resistance
- Mutations
- Function
- The only predicted protein phosphatase in M.tuberculosis, it dephosphorylates at least 5 protein kinases (PknA, PknB, PknD, PknE and PknF) and the penicillin-binding protein PBPA. {ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:14575702, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:16436437}.
- Family
-
Unknown
- GO
-
- integral component of membrane GO:0016021 cellular_component
- phosphoserine phosphatase activity GO:0004647 molecular_function
- protein serine/threonine phosphatase activity GO:0004722 molecular_function
- phosphoprotein phosphatase activity GO:0004721 molecular_function
- negative regulation of DNA binding GO:0043392 biological_process
- negative regulation of protein kinase activity GO:0006469 biological_process
- protein dephosphorylation GO:0006470 biological_process
- integral component of plasma membrane GO:0005887 cellular_component
- cell wall GO:0005618 cellular_component
- manganese ion binding GO:0030145 molecular_function
- negative regulation of catalytic activity GO:0043086 biological_process
- positive regulation of catalytic activity GO:0043085 biological_process
- magnesium ion binding GO:0000287 molecular_function
- InterPro
1TXO
- Name
- PP2C-family Ser/Thr phosphatase (EC 3.1.3.16) (Mycobacterial Ser/Thr phosphatase) (Mstp) (Possible serine/threonine phosphatase Ppp)
- Family
- Unknown
- Protein Sequence
-
MARVTLVLRYAARSDRGLVRANNEDSVYAGARLLALADGMGGHAAGEVASQLVIAALAHLDDDEPGGDLLAKLDAAVRAGNSAIAAQVEMEPDLEGMGTTLTAILFAGNRLGLVHIGDSRGYLLRDGELTQITKDDTFVQTLVDEGRITPEEAHSHPQRSLIMRALTGHEVEPTLTMREARAGDRYLLCSDGLSDPVSDETILEALQIPEVAESAHRLIELALRGGGPDNVTVVVADVVDYDYGQTQPILAGAVSGDDDQLTLPNTAAGRASAISQRKEIVKRVPPQADTFSRPRWSGRRLAFVVALVTVLMTAGLLIGRAIIRSNYYVADYAGSVSIMRGIQGSLLGMSLHQPYLMGCLSPRNELSQISYGQSGGPLDCHLMKLEDLRPPERAQVRAGLPAGTLDDAIGQLRELAANSLLPPCPAPRATSPPGRPAPPTTSETTEPNVTSSPASPSPTTSAPAPTGTTPAIPTSASPAAPASPPTPWPVTSSPTMAALPPPPPQPGIDCRAAA
- Mass
- 53,812 Da
- Length
- 514 Aa
Summary
Rv0018c doesn't seem to be a targeted by any drug.
Rv0018c doesn't seem to be involved in any pathway.
- An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase.
- Structure. 2004 Nov;12(11):1947-54. doi: 10.1016/j.str.2004.09.008.
- 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.
- targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis.
- BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109.
- The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division.
- Microbiology. 2006 Feb;152(Pt 2):493-504. doi: 10.1099/mic.0.28630-0.
- Conserved autophosphorylation pattern in activation loops and juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein kinases.
- Biochem Biophys Res Commun. 2005 Aug 5;333(3):858-67. doi: 10.1016/j.bbrc.2005.05.173.
- PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis.
- Mol Microbiol. 2003 Sep;49(6):1493-508.
- Phosphoprotein phosphatase of Mycobacterium tuberculosis dephosphorylates serine-threonine kinases PknA and PknB.
- Biochem Biophys Res Commun. 2003 Nov 7;311(1):112-20. doi: 10.1016/j.bbrc.2003.09.173.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.