ID   FAD11_MYCTO             Reviewed;         571 AA.
AC   P9WQ52; L0T9R9; Q10776;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Putative fatty-acid--CoA ligase fadD11;
DE            EC=6.2.1.-;
DE   AltName: Full=Acyl-CoA synthetase;
GN   Name=fadD11; OrderedLocusNames=MT1600;
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45867.1; -; Genomic_DNA.
DR   PIR; C70762; C70762.
DR   RefSeq; WP_003898924.1; NC_002755.2.
DR   AlphaFoldDB; P9WQ52; -.
DR   EnsemblBacteria; AAK45867; AAK45867; MT1600.
DR   KEGG; mtc:MT1600; -.
DR   PATRIC; fig|83331.31.peg.1722; -.
DR   HOGENOM; CLU_000022_45_5_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12780; -; 2.
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   Cell membrane; Fatty acid metabolism; Ligase; Lipid metabolism; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..571
FT                   /note="Putative fatty-acid--CoA ligase fadD11"
FT                   /id="PRO_0000426836"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  62309 MW;  37043842FBC9CD31 CRC64;
     MARLRGAGAA GRCRPGRFGS SARRHGLADD GEPDRVLPAR RRCSARRRHL VFGVQHPARR
     AADLRVRQRG DQGGHLRATV RRSRSRQRCA HRTHRLRRWR APGTLSLTDL YAAASGDFFD
     FESTWRAVQP EDIVTLIYTS GTTGNPKGVE MTHANLLFEG YAIDEVLGIR FGDRVTSFLP
     SAHIADRMTG LYLQEMFGTQ VTAVADARTI AAALPDVRPT VWGAVPRVWE KLKAGIEFTV
     ARETDEMKRQ ALAWAMSVAG KRANALLAGE SMSDQLVAEW AKADELVLSK LRERLGFGEL
     RWALSGAAPI PKETLAFFAG IGIPIAEIWG MSELSCVATA SHPRDGRLGT VGKLLPGLQG
     KIAEDGEYLV RGPLVMKGYR KEPAKTAEAI DSDGWLHTGD VFDIDSDGYL RVVDRKKELI
     INAAGKNMSP ANIENTILAA CPMVGVMMAI GDGRTYNTAL LVFDADSLGP YAAQRGLDAS
     PAALAADPEV IARIAAGVAE GNAKLSRVEQ IKRFRILPTL WEPGGDEITL TMKLKRRRIA
     AKYSAEIEEL YASELRPQVY EPAAVPSTQP A