ID   BUK_BACCQ               Reviewed;         367 AA.
AC   B9IXF8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=BCQ_3951;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM14379.1; -; Genomic_DNA.
DR   RefSeq; WP_000115774.1; NC_011969.1.
DR   AlphaFoldDB; B9IXF8; -.
DR   SMR; B9IXF8; -.
DR   EnsemblBacteria; ACM14379; ACM14379; BCQ_3951.
DR   GeneID; 64199515; -.
DR   KEGG; bcq:BCQ_3951; -.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; IWHALNQ; -.
DR   Proteomes; UP000000441; 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_1000146588"
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