ID   BUK_CLOBB               Reviewed;         355 AA.
AC   B2TIN4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=CLL_A0297;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-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; CP001056; ACD21995.1; -; Genomic_DNA.
DR   RefSeq; WP_012422882.1; NC_018648.1.
DR   AlphaFoldDB; B2TIN4; -.
DR   SMR; B2TIN4; -.
DR   EnsemblBacteria; ACD21995; ACD21995; CLL_A0297.
DR   KEGG; cbk:CLL_A0297; -.
DR   PATRIC; fig|935198.13.peg.272; -.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; ANDEGPF; -.
DR   OrthoDB; 537106at2; -.
DR   Proteomes; UP000001195; 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..355
FT                   /note="Probable butyrate kinase"
FT                   /id="PRO_1000128903"
SQ   SEQUENCE   355 AA;  38536 MW;  FE62875066AFDD89 CRC64;
     MSYKLLIINP GSTSTKIGVY ENEKELFEET LRHTNEEIKR YETIYDQFQF RKDVILNILK
     EKNFDITTLS AIVGRGGMLK PVEGGTYAVN DAMIEDLKVG VQGPHASNLG GIIAKSIGDE
     LNIPSFIVDP VVTDELDDVA RLSGVPELPR KSKFHALNQK AVAKRYGKDS GKGYENLNLI
     VVHMGGGVSV GAHKQGKVVD VNNALDGDGP FSPERAGTVP VGDLIKMCFS GQYTESEVYT
     KVVGKGGFVG YLNTNDVKGV IDNMEAGDKD CEKIYKAFLY QITKTIGEMA AALNGKVDQI
     LLTGGIAYSP TLVPDLKSNV EWIAPVTVYP GEDELLALAQ GAIRVLDGEE KAKIY