MBTM_MYCTU
ID MBTM_MYCTU Reviewed; 521 AA.
AC P9WQ41; L0T9C8; P0A4X8; Q11015;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase MbtM {ECO:0000305};
DE EC=6.2.1.20 {ECO:0000250|UniProtKB:A0QUA1};
DE EC=6.2.1.47 {ECO:0000269|PubMed:16461464};
DE AltName: Full=Fatty acyl-[acyl-carrier-protein] synthetase;
DE Short=Fatty acyl-ACP synthetase;
DE AltName: Full=Mycobactin synthetase protein M;
GN Name=mbtM {ECO:0000303|PubMed:16461464};
GN Synonyms=fadD33 {ECO:0000303|PubMed:12065475}; OrderedLocusNames=Rv1345;
GN ORFNames=MTCY02B10.09;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12065475; DOI=10.1128/iai.70.7.3371-3381.2002;
RA Rodriguez G.M., Voskuil M.I., Gold B., Schoolnik G.K., Smith I.;
RT "IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in
RT iron-dependent gene expression, iron metabolism, and oxidative stress
RT response.";
RL Infect. Immun. 70:3371-3381(2002).
RN [3]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12480891; DOI=10.1099/00221287-148-12-3873;
RA Rindi L., Fattorini L., Bonanni D., Iona E., Freer G., Tan D., Deho G.,
RA Orefici G., Garzelli C.;
RT "Involvement of the fadD33 gene in the growth of Mycobacterium tuberculosis
RT in the liver of BALB/c mice.";
RL Microbiology 148:3873-3880(2002).
RN [4]
RP FUNCTION, ROLE IN MYCOBACTIN BIOSYNTHESIS, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16461464; DOI=10.1073/pnas.0507924103;
RA Krithika R., Marathe U., Saxena P., Ansari M.Z., Mohanty D., Gokhale R.S.;
RT "A genetic locus required for iron acquisition in Mycobacterium
RT tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2069-2074(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Activates lipidic moieties required for mycobactin
CC biosynthesis (PubMed:16461464). Converts medium- to long-chain
CC aliphatic fatty acids into acyl adenylate, which is further transferred
CC on to the phosphopantetheine arm of the carrier protein MbtL
CC (PubMed:16461464). {ECO:0000269|PubMed:16461464}.
CC -!- FUNCTION: May play a role in virulence by supporting bacterial growth
CC in the liver. {ECO:0000269|PubMed:12480891}.
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:0000269|PubMed:16461464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dodecanoate + holo-[ACP] = AMP + diphosphate +
CC dodecanoyl-[ACP]; Xref=Rhea:RHEA:63620, Rhea:RHEA-COMP:9644,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:16461464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63621;
CC Evidence={ECO:0000269|PubMed:16461464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dodecanoate + H(+) = diphosphate + dodecanoyl-AMP;
CC Xref=Rhea:RHEA:43712, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83623;
CC Evidence={ECO:0000269|PubMed:16461464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43713;
CC Evidence={ECO:0000269|PubMed:16461464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-AMP + holo-[ACP] = AMP + dodecanoyl-[ACP] + H(+);
CC Xref=Rhea:RHEA:46504, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264,
CC ChEBI:CHEBI:83623, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:16461464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46505;
CC Evidence={ECO:0000269|PubMed:16461464};
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC {ECO:0000269|PubMed:16461464}.
CC -!- INDUCTION: Induced by iron starvation conditions. Transcriptionally
CC repressed by IdeR and iron. {ECO:0000269|PubMed:12065475}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene decreases growth in the
CC liver, but not in the lungs or spleen. {ECO:0000269|PubMed:12480891}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44103.1; -; Genomic_DNA.
DR PIR; H70739; H70739.
DR RefSeq; NP_215861.1; NC_000962.3.
DR RefSeq; WP_003406950.1; NZ_NVQJ01000031.1.
DR AlphaFoldDB; P9WQ41; -.
DR SMR; P9WQ41; -.
DR STRING; 83332.Rv1345; -.
DR SwissLipids; SLP:000001253; -.
DR PaxDb; P9WQ41; -.
DR DNASU; 886855; -.
DR GeneID; 45425323; -.
DR GeneID; 886855; -.
DR KEGG; mtu:Rv1345; -.
DR TubercuList; Rv1345; -.
DR eggNOG; COG0318; Bacteria.
DR OMA; FRWLTWL; -.
DR PhylomeDB; P9WQ41; -.
DR BioCyc; MetaCyc:G185E-5524-MON; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0070566; F:adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IDA:MTBBASE.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
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_0000193141"
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
