ID   BUK_BACC7               Reviewed;         367 AA.
AC   B7HNS7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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};
GN   OrderedLocusNames=BCAH187_A4294;
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001177; ACJ79148.1; -; Genomic_DNA.
DR   RefSeq; WP_000115774.1; NC_011658.1.
DR   AlphaFoldDB; B7HNS7; -.
DR   SMR; B7HNS7; -.
DR   EnsemblBacteria; ACJ79148; ACJ79148; BCAH187_A4294.
DR   GeneID; 64199515; -.
DR   KEGG; bcr:BCAH187_A4294; -.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; IWHALNQ; -.
DR   OrthoDB; 537106at2; -.
DR   Proteomes; UP000002214; 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_1000128900"
SQ   SEQUENCE   367 AA;  40010 MW;  40B1E4BB62371422 CRC64;
     MSVNRILVIN PGSTSTKIGV FDNERPVLEE TIRHDEEQIG KYKRIIDQYE FRKETILEVL
     HSHGINISKL NAVCGRGGLL RPIEGGTYTV NDAMLEDLKN GFSGHHASNL GGILAYEIAS
     GLNIPAFIVD PVVVDEMEPI ARISGIAGME RKSIFHALNQ KAVARKVAEQ LNHKYEDLNL
     LVTHMGGGIT VGAHKKGRVI DVNNGLNGEG PFSPERAGTV PVGQLVEMCF SGEYYRDEMI
     KKLVGQGGLV SLIGTNDAIK VEQMVEKGDP EATLIYKAMA YQVAKEIGGA SAVLHGKIDA
     IVLTGGLAYS KILVDEIKER VDWIADVIVH PGEDELQALA EGALRVLREE EAPKEYIVRE
     KETVARG