ID   BUK_BACC1               Reviewed;         367 AA.
AC   Q731D0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Probable butyrate kinase {ECO:0000255|HAMAP-Rule:MF_00542};
DE            Short=BK {ECO:0000255|HAMAP-Rule:MF_00542};
DE            EC=2.7.2.7 {ECO:0000255|HAMAP-Rule:MF_00542};
DE   AltName: Full=Branched-chain carboxylic acid kinase {ECO:0000255|HAMAP-Rule:MF_00542};
GN   Name=buk {ECO:0000255|HAMAP-Rule:MF_00542}; OrderedLocusNames=BCE_4236;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + butanoate = ADP + butanoyl phosphate;
CC         Xref=Rhea:RHEA:13585, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58079, ChEBI:CHEBI:456216; EC=2.7.2.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00542};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00542}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00542}.
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DR   EMBL; AE017194; AAS43137.1; -; Genomic_DNA.
DR   RefSeq; WP_000056191.1; NC_003909.8.
DR   AlphaFoldDB; Q731D0; -.
DR   SMR; Q731D0; -.
DR   EnsemblBacteria; AAS43137; AAS43137; BCE_4236.
DR   GeneID; 59155261; -.
DR   KEGG; bca:BCE_4236; -.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; IWHALNQ; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047761; F:butyrate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00542; Butyrate_kinase; 1.
DR   InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR   InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR011245; Butyrate_kin.
DR   PANTHER; PTHR21060; PTHR21060; 1.
DR   PANTHER; PTHR21060:SF3; PTHR21060:SF3; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF036458; Butyrate_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02707; butyr_kinase; 1.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..367
FT                   /note="Probable butyrate kinase"
FT                   /id="PRO_1000061063"
SQ   SEQUENCE   367 AA;  39969 MW;  10D55D7011B529F6 CRC64;
     MSLNRILVIN PGSTSTKIGV FDNERPVLEE TIRHDEEQIG KYKRIIDQYE FRKETILEVL
     HSHGINISKL NAVCGRGGLL RPIEGGTYTV NDAMLEDLKN GFSGHHASNL GGILAYEIAS
     GLNIPAFIVD PVVVDEMEPV ARISGIAGME RKSIFHALNQ KAVARKVAEE LNHKYEDLNL
     LVTHMGGGIT VGAHKKGKVI DVNNGLNGEG PFSPERAGTV PVGQLVEMCF SGEYYRDEMV
     KKLVGQGGLV SLIGTNDAIK VEQMVEKGDP EATLIYKAMA YQVAKEIGGA SAVLHGKIDA
     IVLTGGLAYS KILVDEIKER VDWIADVIVH PGEDELQALA EGALRVLREE EAPKEYIVRE
     KETVARG