ID   BUK_ENTFA               Reviewed;         360 AA.
AC   Q9RPS7;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=EF_1662;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX   PubMed=10464218; DOI=10.1128/jb.181.17.5433-5442.1999;
RA   Ward D.E., Ross R.P., van der Weijden C.C., Snoep J.L., Claiborne A.;
RT   "Catabolism of branched-chain alpha-keto acids in Enterococcus faecalis:
RT   the bkd gene cluster, enzymes, and metabolic route.";
RL   J. Bacteriol. 181:5433-5442(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AF149712; AAD55375.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO81440.1; -; Genomic_DNA.
DR   RefSeq; NP_815370.1; NC_004668.1.
DR   RefSeq; WP_002369343.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q9RPS7; -.
DR   SMR; Q9RPS7; -.
DR   STRING; 226185.EF_1662; -.
DR   EnsemblBacteria; AAO81440; AAO81440; EF_1662.
DR   KEGG; efa:EF1662; -.
DR   PATRIC; fig|226185.45.peg.1849; -.
DR   eggNOG; COG3426; Bacteria.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; IWHALNQ; -.
DR   Proteomes; UP000001415; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..360
FT                   /note="Probable butyrate kinase"
FT                   /id="PRO_0000107669"
FT   CONFLICT        48
FT                   /note="S -> P (in Ref. 1; AAD55375)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64
FT                   /note="I -> T (in Ref. 1; AAD55375)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="S -> T (in Ref. 1; AAD55375)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        317
FT                   /note="V -> I (in Ref. 1; AAD55375)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  39256 MW;  A20F08DFC375C3CF CRC64;
     METVLVINPG STSTKLALFA NHDCLAEETL RHSVQELAPF ENVVSQTSFR KQMIAEFLET
     HNIIQLAAVV GRGGLLKPIP GGTYLVDQQM LEDLRTERFN THASNLGAIL ANEFAEKYHV
     PAFIVDPVVV DELQPLARIS GLKGIQRRSV GHALNQKAVA RKIAEDLGKT YEQSNFIVVH
     LGGGISLGAH QKGRMVDVVN GLDGEGPYTP ERSGALPLVE FAQWILEQEL TISQVKKLIA
     GNSGLKSYLG ETDLRHIQAQ IAAGDQTANY YLKGMCYQIA KSIGEMAVVL EGTIDAIILT
     GGAAYSQTVV QEISQKVTWI APIKVYPGEM EMAALYEGVN RVLTGEEQAL NYSEAKIEQE