(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 106.
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}.
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   SMR; P54530; -.
DR   STRING; 224308.BSU24090; -.
DR   PaxDb; P54530; -.
DR   PRIDE; P54530; -.
DR   DNASU; 938671; -.
DR   EnsemblBacteria; CAB14340; CAB14340; BSU24090.
DR   GeneID; 938671; -.
DR   KEGG; bsu:BSU24090; -.
DR   PATRIC; fig|224308.179.peg.2623; -.
DR   eggNOG; COG0280; LUCA.
DR   HOGENOM; HOG000009438; -.
DR   InParanoid; P54530; -.
DR   KO; K00634; -.
DR   OMA; HCVRVAN; -.
DR   PhylomeDB; P54530; -.
DR   BioCyc; BSUB:BSU24090-MONOMER; -.
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;
DR   PRODOM; P54530.
DR   SWISS-2DPAGE; P54530.
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
//

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