ID   MBTM_MYCBO              Reviewed;         521 AA.
AC   P0A4X9; A0A1R3Y073; Q11015; X2BHE8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase MbtM {ECO:0000250|UniProtKB:A0QUA1};
DE            EC=6.2.1.20 {ECO:0000250|UniProtKB:A0QUA1};
DE            EC=6.2.1.47 {ECO:0000250|UniProtKB:A0QUA1};
DE   AltName: Full=Fatty acyl-[acyl-carrier-protein] synthetase {ECO:0000250|UniProtKB:A0QUA1};
DE            Short=Fatty acyl-ACP synthetase {ECO:0000250|UniProtKB:A0QUA1};
DE   AltName: Full=Mycobactin synthetase protein M {ECO:0000250|UniProtKB:A0QUA1};
GN   Name=mbtM; Synonyms=fadD33; OrderedLocusNames=BQ2027_MB1380;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Activates lipidic moieties required for mycobactin
CC       biosynthesis. Converts medium- to long-chain aliphatic fatty acids into
CC       acyl adenylate, which is further transferred on to the
CC       phosphopantetheine arm of the carrier protein MbtL.
CC       {ECO:0000250|UniProtKB:A0QUA1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC         fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC         Evidence={ECO:0000250|UniProtKB:A0QUA1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + holo-[ACP] = a medium-chain
CC         fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:50460,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12681, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59558, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:133242, ChEBI:CHEBI:456215; EC=6.2.1.47;
CC         Evidence={ECO:0000250|UniProtKB:A0QUA1};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000250|UniProtKB:A0QUA1}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT708304; SIT99983.1; -; Genomic_DNA.
DR   RefSeq; NP_855034.1; NC_002945.3.
DR   RefSeq; WP_003406950.1; NC_002945.4.
DR   AlphaFoldDB; P0A4X9; -.
DR   SMR; P0A4X9; -.
DR   EnsemblBacteria; SIT99983; SIT99983; BQ2027_MB1380.
DR   GeneID; 45425323; -.
DR   PATRIC; fig|233413.5.peg.1512; -.
DR   OMA; FRWLTWL; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   CDD; cd05931; FAAL; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..521
FT                   /note="Medium/long-chain-fatty-acid--[acyl-carrier-protein]
FT                   ligase MbtM"
FT                   /id="PRO_0000193140"
SQ   SEQUENCE   521 AA;  53957 MW;  2D432512077122DB CRC64;
     MSELAAVLTR SMQASAGDLM VLDRETSLWC RHPWPEVHGL AESVAAWLLD HDRPAAVGLV
     GEPTVELVAA IQGAWLAGAA VSILPGPVRG ANDQRWADAT LTRFLGIGVR TVLSQGSYLA
     RLRSVDTAGV TIGDLSTAAH TNRSATPVAS EGPAVLQGTA GSTGAPRTAI LSPGAVLSNL
     RGLNQRVGTD AATDVGCSWL PLYHDMGLAF VLSAALAGAP LWLAPTTAFT ASPFRWLSWL
     SDSGATMTAA PNFAYNLIGK YARRVSEVDL GALRVTLNGG EPVDCDGLTR FAEAMAPFGF
     DAGAVLPSYG LAESTCAVTV PVPGIGLLAD RVIDGSGAHK HAVLGNPIPG MEVRISCGDQ
     AAGNASREIG EIEIRGASMM AGYLGQQPID PDDWFATGDL GYLGAGGLVV CGRAKEVISI
     AGRNIFPTEV ELVAAQVRGV REGAVVALGT GDRSTRPGLV VAAEFRGPDE ANARAELIQR
     VASECGIVPS DVVFVSPGSL PRTSSGKLRR LAVRRSLEMA D