YHFT_BACSU
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 03-AUG-2022, entry version 111.
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; Firmicutes; 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; O07619; -.
DR PRIDE; O07619; -.
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 OMA; WFESVCK; -.
DR PhylomeDB; O07619; -.
DR BioCyc; BSUB:BSU10360-MON; -.
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 Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 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