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Database: UniProt
Entry: A0A147K7X4_9BACI
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ID   A0A147K7X4_9BACI        Unreviewed;       367 AA.
AC   A0A147K7X4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Probable butyrate kinase {ECO:0000256|HAMAP-Rule:MF_00542};
DE            Short=BK {ECO:0000256|HAMAP-Rule:MF_00542};
DE            EC=2.7.2.7 {ECO:0000256|HAMAP-Rule:MF_00542};
DE   AltName: Full=Branched-chain carboxylic acid kinase {ECO:0000256|HAMAP-Rule:MF_00542};
GN   Name=buk {ECO:0000256|HAMAP-Rule:MF_00542};
GN   ORFNames=Q75_09485 {ECO:0000313|EMBL:KUP06157.1};
OS   Bacillus coahuilensis p1.1.43.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP06157.1, ECO:0000313|Proteomes:UP000074108};
RN   [1] {ECO:0000313|EMBL:KUP06157.1, ECO:0000313|Proteomes:UP000074108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX   PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA   Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA   Olmedo-Alvarez G.;
RT   "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT   Phosphorus Acquisition Strategies and Their Regulation.";
RL   Front. Microbiol. 7:58-58(2016).
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:0000256|ARBA:ARBA00001819, ECO:0000256|HAMAP-
CC         Rule:MF_00542};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00542}.
CC   -!- SIMILARITY: Belongs to the acetokinase family.
CC       {ECO:0000256|ARBA:ARBA00008748, ECO:0000256|HAMAP-Rule:MF_00542,
CC       ECO:0000256|RuleBase:RU003835}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUP06157.1}.
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DR   EMBL; LDYG01000030; KUP06157.1; -; Genomic_DNA.
DR   RefSeq; WP_059351212.1; NZ_LDYG01000030.1.
DR   AlphaFoldDB; A0A147K7X4; -.
DR   STRING; 1150625.Q75_09485; -.
DR   PATRIC; fig|1150625.3.peg.2017; -.
DR   OrthoDB; 9771859at2; -.
DR   Proteomes; UP000074108; Unassembled WGS sequence.
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   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02707; butyr_kinase; 1.
DR   PANTHER; PTHR21060; ACETATE KINASE; 1.
DR   PANTHER; PTHR21060:SF3; BUTYRATE KINASE 2-RELATED; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF036458; Butyrate_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00542};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00542};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00542};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00542}; Reference proteome {ECO:0000313|Proteomes:UP000074108};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00542}.
SQ   SEQUENCE   367 AA;  39655 MW;  40C2B33A8A5EC2F5 CRC64;
     MQEQFRILVI NPGSTSTKIG VFDNDDVVFE KTLRHDSDEI NQYPSIIDQY EFRKTTILHA
     LDEEGINVSK LSAVCGRGGL LRPIEGGTYE VNEQMLQDLR KGYSGQHASN LGGIIANEIA
     GALNIPSFIV DPVVVDELSD VARVSGFSLI ERKSIFHALN QKAVARRVAK ELNKSYEELN
     LIVTHMGGGI TVGAHKGGKV IDVNNGLHGD GPFSPERAGT VPAGDLVDLC FSGDFYRDEI
     IKKLVGQGGL VGYLGTNDAI QVEKRIEKGD RKSKLVYDAM AYQVAKEIGS ASAVLQGQVD
     AIILTGGLAY GKDFVSTIVQ QVSWIADVMV KPGENELQAL AEGALRVITG EEKAKVYPNQ
     VKTGLNV
//
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