BUK_BACCN
ID BUK_BACCN Reviewed; 367 AA.
AC A7GSI3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Bcer98_2858;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS23091.1; -; Genomic_DNA.
DR RefSeq; WP_012095318.1; NC_009674.1.
DR AlphaFoldDB; A7GSI3; -.
DR SMR; A7GSI3; -.
DR STRING; 315749.Bcer98_2858; -.
DR EnsemblBacteria; ABS23091; ABS23091; Bcer98_2858.
DR GeneID; 56418402; -.
DR KEGG; bcy:Bcer98_2858; -.
DR eggNOG; COG3426; Bacteria.
DR HOGENOM; CLU_048716_0_0_9; -.
DR OMA; IWHALNQ; -.
DR OrthoDB; 537106at2; -.
DR Proteomes; UP000002300; 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; Transferase.
FT CHAIN 1..367
FT /note="Probable butyrate kinase"
FT /id="PRO_1000081939"
SQ SEQUENCE 367 AA; 39828 MW; 7DCBC9343A3108EC CRC64;
MSVNRILVIN PGSTSTKIGV FDNERPVLEE TIRHDTGEIK KYKRIIDQYE FRKETILEIL
HSHGINISKL SAVCGRGGLL RPIEGGTYTV NEAMLEDLKN GYSGHHASNL GGILAYEIAS
GLNIPAFIVD PVVVDEMEPI ARISGIAGME RKSIFHALNQ KAVARKVAAE IGHKYEDLNL
IIAHMGGGIT VGAHKNGKVI DVNNGLNGEG PFSPERAGTV PVGQLIEMCF SGNYYRDEMM
KKIVGQGGLV SLIGTNDAIK VENMVEKGDP EATLIYKAMA YQVAKEIGGA SAVLHGKIDA
IVLTGGLAYS KILINEIKER VNWIADVIVH PGEDELQALA EGALRVLREE EAPKEYVVRE
KETVARG