ID   BUK_ELUMP               Reviewed;         370 AA.
AC   B2KEH0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Emin_1366;
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191;
RX   PubMed=19270133; DOI=10.1128/aem.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(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; CP001055; ACC98916.1; -; Genomic_DNA.
DR   RefSeq; WP_012415531.1; NC_010644.1.
DR   AlphaFoldDB; B2KEH0; -.
DR   SMR; B2KEH0; -.
DR   STRING; 445932.Emin_1366; -.
DR   EnsemblBacteria; ACC98916; ACC98916; Emin_1366.
DR   KEGG; emi:Emin_1366; -.
DR   HOGENOM; CLU_048716_0_0_0; -.
DR   OMA; IWHALNQ; -.
DR   OrthoDB; 537106at2; -.
DR   Proteomes; UP000001029; 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; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..370
FT                   /note="Probable butyrate kinase"
FT                   /id="PRO_1000128905"
SQ   SEQUENCE   370 AA;  40599 MW;  AF649460C1BECA7F CRC64;
     MEHNILVINP GSTSDDIGYY KGPKTVFEES ARYSQEELDS FAGKELSEQI PLRRKFLLDV
     LKKHEINLNE IDAVIGRGGL LKHIEGGIYT INEAMLADLK RGYNGHHPSN LGGILAREIA
     ESLGKPCFIA DPVVVDEMEP LARYTGFKEI KRKSIFHALN QKRVAITAAK ELGKKYKECN
     FIVMHGGGGV SVGAHKKGKV IDVSDGFEGA GPMTPQRSGV LPSLELVEMC FSGQYTIQEL
     RKKMRGRGGM IAHTGTSDIA DLYNYISSGK KKPGSTINCS REAAQEAFDA MIYQISKEIG
     AMATVLKGDV DAIILTGGLA YNEYLVNMIK ERTGFITDKF FVYPGGDEKA ALKEAAARAL
     ENPEIIKQYK