BUK_CLOPS
ID BUK_CLOPS Reviewed; 356 AA.
AC Q0SQK0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=CPR_2342;
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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; CP000312; ABG86354.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0SQK0; -.
DR SMR; Q0SQK0; -.
DR EnsemblBacteria; ABG86354; ABG86354; CPR_2342.
DR KEGG; cpr:CPR_2342; -.
DR OMA; IWHALNQ; -.
DR Proteomes; UP000001824; 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..356
FT /note="Probable butyrate kinase"
FT /id="PRO_1000061067"
SQ SEQUENCE 356 AA; 38702 MW; 43D4F1A61038D27F CRC64;
MAYKLLIINP GSTSTKIGVY EGEKEILEET LRHSAEEILK YDTIFDQLDF RKEVILKVLK
EKGIDINELD AVVGRGGMLK PIEGGTYEVN EAMVEDLKIG VQGPHASNLG GILSNEIAKE
IGKRAFIVDP VVVDEMEDVA RLSGVPELPR KSKFHALNQK AVAKRYAKEH NTSYEDVNLI
VVHMGGGVSV GAHRKGRVID VNNALDGDGP FSPERAGGVP SGELLEMCFS GKYSKEEVYK
KLVGKGGFVA YANTNDARDL IKLSQEGDEK GSLIFNAFIY QIAKEIGSMA VVLDGEVNAI
VLTGGIAYSD YVTNAINKKV KWIAPMVVYG GEDELLALAQ GAIRVLDGVE EAKIYK