PTB_BACSU
ID PTB_BACSU Reviewed; 299 AA.
AC P54530;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable phosphate butyryltransferase;
DE EC=2.3.1.19;
DE AltName: Full=Phosphotransbutyrylase;
GN Name=yqiS; OrderedLocusNames=BSU24090;
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 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
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 SEQUENCE REVISION TO 234.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- FUNCTION: Catalyzes the conversion of butyryl-CoA through butyryl
CC phosphate to butyrate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + phosphate = butanoyl phosphate + CoA;
CC Xref=Rhea:RHEA:20892, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:58079; EC=2.3.1.19;
CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC butyryltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D84432; BAA12594.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14340.2; -; Genomic_DNA.
DR PIR; A69962; A69962.
DR RefSeq; NP_390289.2; NC_000964.3.
DR RefSeq; WP_004398694.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54530; -.
DR SMR; P54530; -.
DR STRING; 224308.BSU24090; -.
DR PaxDb; P54530; -.
DR PRIDE; P54530; -.
DR DNASU; 938671; -.
DR EnsemblBacteria; CAB14340; CAB14340; BSU_24090.
DR GeneID; 938671; -.
DR KEGG; bsu:BSU24090; -.
DR PATRIC; fig|224308.179.peg.2623; -.
DR eggNOG; COG0280; Bacteria.
DR InParanoid; P54530; -.
DR OMA; CIVDGPF; -.
DR PhylomeDB; P54530; -.
DR BioCyc; BSUB:BSU24090-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0050182; F:phosphate butyryltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019605; P:butyrate metabolic process; IEA:InterPro.
DR InterPro; IPR012147; P_Ac_Bu_trans.
DR InterPro; IPR014079; Phosphate_butyryltransferase.
DR InterPro; IPR002505; PTA_PTB.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF000428; P_Ac_trans; 1.
DR TIGRFAMs; TIGR02706; P_butyryltrans; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="Probable phosphate butyryltransferase"
FT /id="PRO_0000179154"
FT CONFLICT 234
FT /note="A -> P (in Ref. 1; BAA12594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 31747 MW; 0D873919C0C6CA5A CRC64;
MKLKDLIGKA SIHKNKTIAV AHAEDEEVIR AVKLAAEHLS ARFLLTGDSK KLNELTSSMQ
GHQVEIVHAN TPEESAKLAV RAVHHKTADV LMKGNVPTSV LLKAVLNRQE GLRSASVLSH
VAVFDIPDFD RLMFVTDSAM NIAPSLEELR QILQNAVHVA HAVGNNMPKA AALAAVETVN
PKMEATVNAA ALAQMYKRGQ IKGCIVDGPL ALDNAVSQIA AAQKKISGDV AGNADILLVP
TIEAGNILYK SLIYFAKASV AAVITGAKAP IALTSRADSA ENKLYSIALA ICASEEYTH
