ID   BUK_CLOPE               Reviewed;         356 AA.
AC   P0C2D8; Q9ZNE5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Butyrate kinase;
DE            Short=BK;
DE            EC=2.7.2.7;
GN   Name=buk; Synonyms=bukA; OrderedLocusNames=CPE2347;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- FUNCTION: Catalyzes the conversion of butyryl-CoA through butyryl
CC       phosphate to butyrate. {ECO:0000250}.
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   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000305}.
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DR   EMBL; BA000016; BAB82053.1; -; Genomic_DNA.
DR   RefSeq; WP_011010889.1; NC_003366.1.
DR   AlphaFoldDB; P0C2D8; -.
DR   SMR; P0C2D8; -.
DR   STRING; 195102.gene:10491664; -.
DR   EnsemblBacteria; BAB82053; BAB82053; BAB82053.
DR   KEGG; cpe:CPE2347; -.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; IWHALNQ; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000000818; 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:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..356
FT                   /note="Butyrate kinase"
FT                   /id="PRO_0000107660"
SQ   SEQUENCE   356 AA;  38645 MW;  9B704B2BC3DAD020 CRC64;
     MAYKLLIINP GSTSTKIGVY EGEKEVLEET LRHSAEEILK YATIFDQLDF RKEVILKVLK
     EKGIDINELD AVVGRGGMLK PIEGGTYEVN EAMVEDLKIG VQGPHASNLG GILSNEIAKE
     IGKRAFIVDP VVVDEMEDVA RLSGVPELPR KSKFHALNQK AVAKRYAKEH NTSYEDVNLI
     VVHMGGGVSV GAHRKGRVID VNNALDGDGP FSPERAGGVP SGELLEMCFS GKYSKEEVYK
     KLVGKGGFVA YANTNDARDL IKLSQEGDEK GSLIFNAFIY QIAKEIGSMA VVLDGEVDAI
     VLTGGIAYSD YVTNAINKKV KWIAPMVVYG GEDELLALAQ GAIRVLDGVE EAKIYK