ID   BUK_CLOTE               Reviewed;         356 AA.
AC   Q890U0;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Butyrate kinase;
DE            Short=BK {ECO:0000255|HAMAP-Rule:MF_00542};
DE            EC=2.7.2.7 {ECO:0000255|HAMAP-Rule:MF_00542};
GN   Name=buk {ECO:0000255|HAMAP-Rule:MF_00542}; OrderedLocusNames=CTC_02545;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00542};
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
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; AE015927; AAO37005.1; -; Genomic_DNA.
DR   RefSeq; WP_011100666.1; NC_004557.1.
DR   AlphaFoldDB; Q890U0; -.
DR   SMR; Q890U0; -.
DR   STRING; 212717.CTC_02545; -.
DR   EnsemblBacteria; AAO37005; AAO37005; CTC_02545.
DR   GeneID; 64180001; -.
DR   KEGG; ctc:CTC_02545; -.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; IWHALNQ; -.
DR   OrthoDB; 537106at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001412; 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_0000107662"
SQ   SEQUENCE   356 AA;  38901 MW;  129E68B567BA4FDC CRC64;
     MAHKLLIINP GSTSTKIGVF EDENLIFEET LRHSAEEIGK YSNVYEQFPF RKEVILNVLK
     EKGFDINTLD AIVGRGGLLK PVEGGTYEVN DAMLKDLRES VRGEHASNLG GIIGNEIAKS
     LNIPAFIVDP VVVDELQDIA RISGMPEIER TSIFHALNQK AVARRYAKEN NKSYEDVNIV
     VVHMGGGSSV GAHKNGKIID VNNALDGEGP FSPERSGGVP IGDLVRLCYS GKYTLDEIIK
     KINGKGGAVA YLGTNDFREV EEKALAGDEK YKLILDAFIY QISKEIGKCS VVLEGNVDAI
     VLTGGIAYSK YVTKEIENKV KFIAPVVLYP GEDELLALTQ GGLRVLNGEE KAKEYK