YHFS_BACSU
ID YHFS_BACSU Reviewed; 364 AA.
AC O07618; Q796T4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative acetyl-CoA C-acetyltransferase YhfS;
DE EC=2.3.1.-;
GN Name=yhfS; OrderedLocusNames=BSU10350;
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;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
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 thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; Y14084; CAA74542.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12875.1; -; Genomic_DNA.
DR PIR; H69831; H69831.
DR RefSeq; NP_388916.1; NC_000964.3.
DR RefSeq; WP_003233154.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07618; -.
DR SMR; O07618; -.
DR STRING; 224308.BSU10350; -.
DR PaxDb; O07618; -.
DR PRIDE; O07618; -.
DR EnsemblBacteria; CAB12875; CAB12875; BSU_10350.
DR GeneID; 939311; -.
DR KEGG; bsu:BSU10350; -.
DR PATRIC; fig|224308.179.peg.1113; -.
DR eggNOG; COG0183; Bacteria.
DR InParanoid; O07618; -.
DR OMA; DIIMGCV; -.
DR PhylomeDB; O07618; -.
DR BioCyc; BSUB:BSU10350-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..364
FT /note="Putative acetyl-CoA C-acetyltransferase YhfS"
FT /id="PRO_0000360670"
FT ACT_SITE 82
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 364 AA; 38399 MW; 5E61586D3DEED2BA CRC64;
MNAVIVDAKR TIFGNQNGLL KPFLPEDLAA PIIRCLSRKL EDQVDEVILG NATGRGGNLA
RLSALQAGLP LSVPGMTIDR QCGSGLEAVR YACSLIQAGA GTMYIAGGSE SSSQSPFSER
ARFSPDAIGD PDMGIAAEYT AARYSISRSM QDEYALLSHQ RSRNAHDEGF YREEVVALGE
LETDEAFLKT RPIEAIIPRA KPVFDTSSGT VTAANSSGIA DGAAALLVME EEKAAALGLK
PVLRFIGSAV SGIHPNFPPA APVVAIRQLL HTHDVTPDDI DLFEINEAFA VKICVCSQEL
GIPFSKINVR GGALALGHPY GASGAALVTR LFYEAKRRPD CQYAVAAIGS GGGIGLALLF
EVLA