ID   MBTM_MYCTO              Reviewed;         521 AA.
AC   P9WQ40; L0T9C8; P0A4X8; Q11015;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
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=MT1387;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45651.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK45651.1; ALT_FRAME; Genomic_DNA.
DR   PIR; H70739; H70739.
DR   AlphaFoldDB; P9WQ40; -.
DR   SMR; P9WQ40; -.
DR   EnsemblBacteria; AAK45651; AAK45651; MT1387.
DR   KEGG; mtc:MT1387; -.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000001020; 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   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   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_0000426842"
SQ   SEQUENCE   521 AA;  53975 MW;  B963CDB72C89F912 CRC64;
     MSELAAVLTR SMQASAGDLM VLDRETSLWC RHPWPEVHGL AESVCGWLLD 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