ID   MBTM_MYCPA              Reviewed;         521 AA.
AC   Q73ZP7;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=MAP_1554c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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}.
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DR   EMBL; AE016958; AAS03871.1; -; Genomic_DNA.
DR   RefSeq; WP_003877914.1; NC_002944.2.
DR   AlphaFoldDB; Q73ZP7; -.
DR   SMR; Q73ZP7; -.
DR   STRING; 262316.MAP_1554c; -.
DR   EnsemblBacteria; AAS03871; AAS03871; MAP_1554c.
DR   KEGG; mpa:MAP_1554c; -.
DR   PATRIC; fig|262316.17.peg.1646; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   OMA; FRWLTWL; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000000580; 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; Reference proteome.
FT   CHAIN           1..521
FT                   /note="Medium/long-chain-fatty-acid--[acyl-carrier-protein]
FT                   ligase MbtM"
FT                   /id="PRO_0000278304"
FT   REGION          146..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  54332 MW;  887D805A7C877FF9 CRC64;
     MSELAAALTA AMRTGGSDLV VFDRESAAWR RHRWPEVHGL AEGIAAWLLD RDRPAALGLV
     GEPTLEFVAA IVGAWLAGAG VSILPGPVRG AEGRRWADTT LTRFAGIGVR TVLSHGSHLD
     ALQALDPSRP DEMVVEDLAV AANTGRRCPE PPAPHANPAI LQGTAGSTGT PKTAALSPDA
     VLANLRGLNA RLGVTPADVG CSWLPLYHDM GLSFLLASAL GGMSLWLAPT SAFTASPFRW
     LAWLSESRAT ITAAPNFAYN LVGKYARRVS GVDLGALRVA INGGEPVDCA GFERFTTAMA
     PFGFDAGAAT PSYGLAEATC AVSVPAPGTG LRFADVSDET GTRRHAVLGA PIPGTEIRIS
     PRHDAPDGIG EIEIRGASMM DGYLGHAPID HQNWFPTGDL GFFSDDGLVV CGRAKELITL
     AGRNIFPTEI ETVAAQVPGV REGAVVALGT GENSARPGLI IAAEFAGRDR AGARAEVIQR
     VASVCGVVPS DVIFMAPGSL PRTSSGKLRR LDVRRSLEAV D