ID   O51162_BORBU            Unreviewed;       630 AA.
AC   O51162;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   02-SEP-2026, entry version 125.
DE   SubName: Full=Long-chain-fatty-acid CoA ligase {ECO:0000313|EMBL:AAC66529.1};
GN   OrderedLocusNames=BB_0137 {ECO:0000313|EMBL:AAC66529.1};
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC   Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326 {ECO:0000313|EMBL:AAC66529.1, ECO:0000313|Proteomes:UP000001807};
RN   [1] {ECO:0000313|EMBL:AAC66529.1, ECO:0000313|Proteomes:UP000001807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31
RC   {ECO:0000313|Proteomes:UP000001807};
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R., Lathigra R.,
RA   White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., Dougherty B.,
RA   Tomb J.F., Fleischmann R.D., Richardson D., Peterson J., Kerlavage A.R.,
RA   Quackenbush J., Salzberg S., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J., Weidman J., Utterback T., Watthey L., McDonald L., Artiach P.,
RA   Bowman C., Garland S., Fuji C., Cotton M.D., Horst K., Roberts K.,
RA   Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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DR   EMBL; AE000783; AAC66529.1; -; Genomic_DNA.
DR   PIR; A70117; A70117.
DR   RefSeq; WP_002658199.1; NC_001318.1.
DR   AlphaFoldDB; O51162; -.
DR   STRING; 224326.BB_0137; -.
DR   PaxDb; 224326-BB_0137; -.
DR   EnsemblBacteria; AAC66529; AAC66529; BB_0137.
DR   GeneID; 46847376; -.
DR   KEGG; bbu:BB_0137; -.
DR   PATRIC; fig|224326.49.peg.535; -.
DR   HOGENOM; CLU_000022_45_5_12; -.
DR   OrthoDB; 311554at2; -.
DR   Proteomes; UP000001807; Chromosome.
DR   CDD; cd17640; LC_FACS_like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_synth/lig_dom.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR052987; Chloroplast_AMP-bd_Enzymes.
DR   PANTHER; PTHR43813; ACYL-ACTIVATING ENZYME 16, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR43813:SF1; ACYL-ACTIVATING ENZYME 16, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF23562; AMP-binding_C_3; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:AAC66529.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001807};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        331..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..453
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   630 AA;  70763 MW;  C8F0A4975293BF26 CRC64;
     MSIAKAFFEV ADQQKDKIAQ MYKVCNGYAH VTYGDLKNNV LKLASFLKSI NVKHQDKIFI
     CSENRAEWTV IDFAILSLGA VDIPKGSDVT LFEAEIIFNS VLPSVVILEN LNLLNMFIQI
     KFTVKPIFII IENLNQEDRL KYSDFEIYTY SDCILFGDTL RKDSEIIEIA SKVDSNDMAT
     IIYTSGTTGH PKGVMLSHAN LLYQVSSFSL MVDTHVGQIF MCILPIWHSF QRSFSYNIFL
     KGMVCLFSTI VPRAMLDDIK NVNPHYIAAV PRLWIAIRQN IYKEVSKKPF ISRMIFHFFV
     KAAFLSDICY RVVMGLYPDN GFSLFFPIKK ILGIFGLICA FPFKALGNVL IFNKINKILG
     NNFVVGITGG GSMPLSAVRF FNSIGIELAN AYGLTETSPG VASNKHKKVI IGTCGKILPG
     TVAEIRDIDG NKLKKPGKGI LFVKGPQVML GYYKDKEATC KIIGSDGFLN TGDIAKLSKD
     NVVQIIGREK DTIVLNNGEN VEPAPIEIKL EESALIEKAV VVGQDQKFLG ALILPNFEEI
     NKYLESVGQK IFDANNRRQI IANNIVLKAI NDEIKKLINK ANGFKPFEQI LKFTLLEKPF
     EVGKEMSIKM DIKRSYILNF YKNEIKNLFI
//