mbtA
- Type
- protein_coding
- Name
- mbtA
- Locus Name
-
Rv2384
- Product
-
Bifunctional enzyme MbtA: salicyl-AMP ligase (SAL-AMP ligase) + salicyl-S-ArCP synthetase
- Functional Category
-
Lipid metabolism
- Location
- 2675936..2677633 (+ strand)
- Gene Length
- 1697 bp
- Nucleotides
-
TGCCACCGAAGGCGGCAGATGGCCGCCGACCCAGTCCCGACGGCGGACTGGGTGGCTTTGTACCGTTCCCCGCGGATCGGGCCGCGTCGTACCGGGCGGCCGGCTATTGGTCGGGGCGAACCCTGGACACCGTGCTCTCCGATGCCGCGCGGCGCTGGCCTGACCGCCTCGCGGTGGCCGACGCCGGTGATCGTCCCGGCCACGGCGGCCTCAGTTACGCCGAACTCGACCAGCGGGCCGACCGGGCCGCCGCGGCGCTGCACGGCCTGGGCATCACGCCAGGCGACCGGGTACTGCTCCAGCTGCCAAACGGCTGCCAGTTCGCGGTTGCCCTGTTCGCGTTATTGCGGGCGGGAGCGATCCCAGTGATGTGCCTGCCCGGTCACCGCGCCGCCGAATTGGGCCACTTCGCCGCCGTCAGCGCGGCCACCGGGCTGGTGGTCGCCGATGTGGCCAGCGGGTTCGACTATCGGCCGATGGCGCGCGAACTTGTTGCCGATCACCCCACCCTGCGCCATGTCATCGTCGATGGCGATCCGGGACCGTTCGTGTCGTGGGCGCAGCTGTGCGCCCAGGCCGGCACCGGTTCGCCGGCACCGCCGGCCGATCCCGGATCGCCAGCGCTGCTGCTGGTCTCCGGCGGCACCACTGGCATGCCCAAACTCATTCCACGCACCCACGACGACTACGTGTTCAACGCGACGGCCAGCGCCGCACTCTGTCGGCTTAGCGCCGACGACGTCTATCTGGTGGTGCTGGCCGCCGGCCACAATTTCCCGCTGGCCTGCCCGGGCCTGCTCGGCGCGATGACCGTCGGGGCCACCGCCGTGTTCGCCCCCGATCCCAGCCCGGAGGCCGCCTTCGCCGCCATCGAGCGCCACGGTGTCACCGTCACCGCGTTGGTTCCGGCACTGGCCAAACTGTGGGCCCAATCCTGTGAGTGGGAGCCGGTGACACCGAAGTCACTGCGGTTGTTGCAGGTTGGCGGGTCCAAGCTAGAACCCGAGGACGCTCGCCGGGTACGCACCGCGCTCACCCCGGGCCTGCAGCAGGTGTTCGGCATGGCGGAGGGGCTGCTGAACTTCACCCGCATCGGCGACCCACCCGAAGTGGTGGAGCACACCCAGGGGCGGCCACTATGCCCGGCCGACGAACTGCGCATCGTCAACGCCGATGGTGAGCCGGTGGGGCCCGGGGAGGAAGGCGAACTCTTGGTGCGCGGGCCCTACACGCTGAACGGCTATTTTGCTGCCGAACGCGACAACGAGCGCTGCTTCGATCCGGACGGCTTCTACCGCAGCGGCGACCTGGTCCGCCGCCGCGACGACGGCAATCTGGTGGTCACCGGGCGCGTCAAGGATGTCATCTGCCGTGCGGGAGAAACCATCGCCGCCAGCGACCTCGAAGAACAGCTGCTGAGCCATCCGGCGATCTTCTCGGCCGCGGCGGTGGGACTACCTGACCAGTATCTGGGGGAAAAAATCTGCGCTGCAGTCGTTTTCGCTGGAGCTCCGATTACGCTTGCGGAGTTGAACGGCTACCTTGACCGGCGTGGTGTGGCCGCGCATACGCGACCCGACCAGCTGGTCGCGATGCCGGCGCTGCCCACAACGCCGATCGGGAAGATCGACAAACGAGCGATCGTCCGCCAGCTCGGCATCGCGACGGGTCCCGTGACGACCCAGCGCTGCCATTGA
- Drug Resistance
- Mutations
- Function
- Involved in the initial steps of the mycobactin biosynthetic pathway. Catalyzes the salicylation of the aryl carrier protein (ArCP) domain of MbtB through a two-step reaction. The first step is the ATP-dependent adenylation of salicylate to generate a salicyl-AMP intermediate. The second step is the transfer of this activated salicylate to MbtB to form a salicyl-ArCP domain thioester. {ECO:0000269|PubMed:9831524}.
- Family
-
ATP-dependent AMP-binding enzyme family
- GO
-
- siderophore biosynthetic process GO:0019290 biological_process
- cellular response to iron ion starvation GO:0010106 biological_process
- ATP binding GO:0005524 molecular_function
- acid-thiol ligase activity GO:0016878 molecular_function
- nucleotidyltransferase activity GO:0016779 molecular_function
- InterPro
Summary
- Name
- Salicyl-AMP ligase / salicyl-S-ArCP synthetase (EC 6.2.1.-) (Mycobactin biosynthesis protein MbtA) (Salicyl-AMP ligase) (Sal-AMP ligase) (EC 2.7.7.-) (Salicyl-S-ArCP synthetase)
- Family
- ATP-dependent AMP-binding enzyme family
- Protein Sequence
-
MPPKAADGRRPSPDGGLGGFVPFPADRAASYRAAGYWSGRTLDTVLSDAARRWPDRLAVADAGDRPGHGGLSYAELDQRADRAAAALHGLGITPGDRVLLQLPNGCQFAVALFALLRAGAIPVMCLPGHRAAELGHFAAVSAATGLVVADVASGFDYRPMARELVADHPTLRHVIVDGDPGPFVSWAQLCAQAGTGSPAPPADPGSPALLLVSGGTTGMPKLIPRTHDDYVFNATASAALCRLSADDVYLVVLAAGHNFPLACPGLLGAMTVGATAVFAPDPSPEAAFAAIERHGVTVTALVPALAKLWAQSCEWEPVTPKSLRLLQVGGSKLEPEDARRVRTALTPGLQQVFGMAEGLLNFTRIGDPPEVVEHTQGRPLCPADELRIVNADGEPVGPGEEGELLVRGPYTLNGYFAAERDNERCFDPDGFYRSGDLVRRRDDGNLVVTGRVKDVICRAGETIAASDLEEQLLSHPAIFSAAAVGLPDQYLGEKICAAVVFAGAPITLAELNGYLDRRGVAAHTRPDQLVAMPALPTTPIGKIDKRAIVRQLGIATGPVTTQRCH
- Mass
- 59,281 Da
- Length
- 565 Aa
Rv2384 doesn't seem to be a targeted by any drug.
Rv2384 doesn't seem to be involved in any pathway.
- 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.
- 5'-O-[(N-acyl)sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: an adenylation enzyme required for siderophore biosynthesis of the mycobactins.
- J Med Chem. 2007 Nov 29;50(24):6080-94. doi: 10.1021/jm070905o. Epub 2007 Oct 30.
- Antitubercular nucleosides that inhibit siderophore biosynthesis: SAR of the glycosyl domain.
- J Med Chem. 2006 Dec 28;49(26):7623-35. doi: 10.1021/jm061068d.
- Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis.
- Nat Chem Biol. 2005 Jun;1(1):29-32. doi: 10.1038/nchembio706. Epub 2005 May 24.
- The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages.
- Mol Microbiol. 2001 Nov;42(3):851-65.
- Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin.
- Chem Biol. 1998 Nov;5(11):631-45.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.