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Database: UniProt
Entry: O07619
LinkDB: O07619
Original site: O07619 
ID   YHFT_BACSU              Reviewed;         479 AA.
AC   O07619; Q796T3;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Uncharacterized acyl--CoA ligase YhfT;
DE            EC=6.2.1.-;
GN   Name=yhfT; OrderedLocusNames=BSU10360;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Noback M.A., Terpstra P., Holsappel S., Venema G., Bron S.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INDUCTION, AND PROBABLE OPERON STRUCTURE.
RC   STRAIN=168 / PY79;
RX   PubMed=11717296; DOI=10.1128/jb.183.24.7371-7380.2001;
RA   Lee J.M., Zhang S., Saha S., Santa Anna S., Jiang C., Perkins J.;
RT   "RNA expression analysis using an antisense Bacillus subtilis genome
RT   array.";
RL   J. Bacteriol. 183:7371-7380(2001).
RN   [4]
RP   DISCUSSION OF FUNCTION.
RX   PubMed=12368242; DOI=10.1101/gr.314502;
RA   Rodionov D.A., Mironov A.A., Gelfand M.S.;
RT   "Conservation of the biotin regulon and the BirA regulatory signal in
RT   Eubacteria and Archaea.";
RL   Genome Res. 12:1507-1516(2002).
CC   -!- FUNCTION: May be involved in fatty acid metabolism.
CC   -!- INDUCTION: Repressed by presence of biotin, under control of BirA.
CC       Probably part of the bioY-yhfST operon. {ECO:0000269|PubMed:11717296}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; Y14084; CAA74543.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12876.1; -; Genomic_DNA.
DR   PIR; A69832; A69832.
DR   RefSeq; NP_388917.1; NC_000964.3.
DR   RefSeq; WP_003244910.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O07619; -.
DR   SMR; O07619; -.
DR   STRING; 224308.BSU10360; -.
DR   PaxDb; 224308-BSU10360; -.
DR   EnsemblBacteria; CAB12876; CAB12876; BSU_10360.
DR   GeneID; 936315; -.
DR   KEGG; bsu:BSU10360; -.
DR   PATRIC; fig|224308.179.peg.1114; -.
DR   eggNOG; COG0318; Bacteria.
DR   InParanoid; O07619; -.
DR   OrthoDB; 9757771at2; -.
DR   PhylomeDB; O07619; -.
DR   BioCyc; BSUB:BSU10360-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   CDD; cd17633; AFD_YhfT-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..479
FT                   /note="Uncharacterized acyl--CoA ligase YhfT"
FT                   /id="PRO_0000390293"
FT   BINDING         150..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         462
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   479 AA;  52881 MW;  4F05AB4FA70D4435 CRC64;
     MTITHTYSST AETSPGRVAI QTESEQITYH DWDRLVSQTA NWLRSQPSMP NRVAILLPNS
     LAFLQLFAGA AAAGCTAIPI DTRWSPAECK ERLSISNADL VVTLAFFKNK LTDSQTPVVL
     LDNCMADISE AAADPLPTID PEHPFYMGFT SGSTGKPKAF TRSHRSWMES FTCTETDFSI
     SSDDKVLIPG ALMSSHFLYG AVSTLFLGGT VCLLKKFSPA KAKEWLCRES ISVLYTVPTM
     TDALARIEGF PDSPVKIISS GADWPAESKK KLAAAWPHLK LYDFYGTSEL SFVTFSSPED
     SKRKPHSAGR PFHNVRIEIR NAGGERCQPG EIGKIFVKSP MRFSGYVNGS TPDEWMTVDD
     MGYVDEEGFL YISGRENGMI VYGGLNIFPE EIERVLLACP EVESAAVVGI PDEYWGEIAV
     AVILGNANAR TLKAWCKQKL ASYKIPKKWV FADSLPETSS GKIARSRVKK WLEESVQYK
//
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