UniProtKB - P71716 (MBTA_MYCTU)
Protein
Salicyl-AMP ligase / salicyl-S-ArCP synthetase
Gene
mbtA
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
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.1 Publication
Catalytic activityi
Activity regulationi
Inhibited by salicyl-AMS, an acyl-AMP analog (PubMed:16407990, PubMed:17181146). Also inhibited by 5'-O-[(N-acyl)sulfamoyl]adenosines (PubMed:17967002).3 Publications
Kineticsi
kcat is 42.7 min(-1) for the adenylation reaction.1 Publication
- KM=9 µM for salicylic acid1 Publication
- KM=3.3 µM for salicylic acid1 Publication
- KM=184 µM for ATP1 Publication
: mycobactin biosynthesis Pathwayi
This protein is involved in the pathway mycobactin biosynthesis, which is part of Siderophore biosynthesis.3 PublicationsView all proteins of this organism that are known to be involved in the pathway mycobactin biosynthesis and in Siderophore biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 214 | ATP; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 330 | ATP; via amide nitrogenBy similarity | 1 | |
Binding sitei | 352 | ATP; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 436 | ATPBy similarity | 1 | |
Binding sitei | 451 | ATPBy similarity | 1 | |
Binding sitei | 542 | ATPBy similarity | 1 |
GO - Molecular functioni
- acid-thiol ligase activity Source: UniProtKB
- ATP binding Source: UniProtKB-KW
- nucleotidyltransferase activity Source: UniProtKB
GO - Biological processi
- cellular response to iron ion starvation Source: MTBBASE
- siderophore biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Ligase, Transferase |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-6610-MONOMER |
UniPathwayi | UPA00011 |
Chemistry databases
SwissLipidsi | SLP:000001282 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:mbtA1 Publication Ordered Locus Names:Rv2384Imported |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv2384 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000445644 | 1 – 565 | Salicyl-AMP ligase / salicyl-S-ArCP synthetaseAdd BLAST | 565 |
Proteomic databases
PaxDbi | P71716 |
Expressioni
Inductioni
Induced by iron starvation conditions. Transcriptionally repressed by IdeR and iron.1 Publication
Interactioni
Protein-protein interaction databases
STRINGi | 83332.Rv2384 |
Chemistry databases
BindingDBi | P71716 |
Family & Domainsi
Sequence similaritiesi
Belongs to the ATP-dependent AMP-binding enzyme family.Curated
Phylogenomic databases
eggNOGi | ENOG4108IQC Bacteria COG1021 LUCA |
HOGENOMi | HOG000230011 |
KOi | K04787 |
OMAi | PMSPHDE |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR025110 AMP-bd_C IPR000873 AMP-dep_Synth/Lig IPR042099 AMP-dep_Synthh-like_sf |
Pfami | View protein in Pfam PF00501 AMP-binding, 1 hit PF13193 AMP-binding_C, 1 hit |
i Sequence
Sequence statusi: Complete.
P71716-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPPKAADGRR PSPDGGLGGF VPFPADRAAS YRAAGYWSGR TLDTVLSDAA
60 70 80 90 100
RRWPDRLAVA DAGDRPGHGG LSYAELDQRA DRAAAALHGL GITPGDRVLL
110 120 130 140 150
QLPNGCQFAV ALFALLRAGA IPVMCLPGHR AAELGHFAAV SAATGLVVAD
160 170 180 190 200
VASGFDYRPM ARELVADHPT LRHVIVDGDP GPFVSWAQLC AQAGTGSPAP
210 220 230 240 250
PADPGSPALL LVSGGTTGMP KLIPRTHDDY VFNATASAAL CRLSADDVYL
260 270 280 290 300
VVLAAGHNFP LACPGLLGAM TVGATAVFAP DPSPEAAFAA IERHGVTVTA
310 320 330 340 350
LVPALAKLWA QSCEWEPVTP KSLRLLQVGG SKLEPEDARR VRTALTPGLQ
360 370 380 390 400
QVFGMAEGLL NFTRIGDPPE VVEHTQGRPL CPADELRIVN ADGEPVGPGE
410 420 430 440 450
EGELLVRGPY TLNGYFAAER DNERCFDPDG FYRSGDLVRR RDDGNLVVTG
460 470 480 490 500
RVKDVICRAG ETIAASDLEE QLLSHPAIFS AAAVGLPDQY LGEKICAAVV
510 520 530 540 550
FAGAPITLAE LNGYLDRRGV AAHTRPDQLV AMPALPTTPI GKIDKRAIVR
560
QLGIATGPVT TQRCH
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45172.1 |
RefSeqi | NP_216900.1, NC_000962.3 WP_003412282.1, NZ_NVQJ01000029.1 |
Genome annotation databases
EnsemblBacteriai | AIR15143; AIR15143; LH57_13000 CCP45172; CCP45172; Rv2384 |
GeneIDi | 885833 |
KEGGi | mtu:Rv2384 mtv:RVBD_2384 |
PATRICi | fig|83332.111.peg.2658 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45172.1 |
RefSeqi | NP_216900.1, NC_000962.3 WP_003412282.1, NZ_NVQJ01000029.1 |
3D structure databases
SMRi | P71716 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv2384 |
Chemistry databases
BindingDBi | P71716 |
ChEMBLi | CHEMBL5662 |
SwissLipidsi | SLP:000001282 |
Proteomic databases
PaxDbi | P71716 |
Genome annotation databases
EnsemblBacteriai | AIR15143; AIR15143; LH57_13000 CCP45172; CCP45172; Rv2384 |
GeneIDi | 885833 |
KEGGi | mtu:Rv2384 mtv:RVBD_2384 |
PATRICi | fig|83332.111.peg.2658 |
Organism-specific databases
TubercuListi | Rv2384 |
Phylogenomic databases
eggNOGi | ENOG4108IQC Bacteria COG1021 LUCA |
HOGENOMi | HOG000230011 |
KOi | K04787 |
OMAi | PMSPHDE |
Enzyme and pathway databases
UniPathwayi | UPA00011 |
BioCyci | MTBH37RV:G185E-6610-MONOMER |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR025110 AMP-bd_C IPR000873 AMP-dep_Synth/Lig IPR042099 AMP-dep_Synthh-like_sf |
Pfami | View protein in Pfam PF00501 AMP-binding, 1 hit PF13193 AMP-binding_C, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MBTA_MYCTU | |
Accessioni | P71716Primary (citable) accession number: P71716 Secondary accession number(s): F2GI64, I6Y957, Q7D787 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 7, 2018 |
Last sequence update: | August 1, 1998 | |
Last modified: | November 13, 2019 | |
This is version 133 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways