ID   BUK2_CLOAB              Reviewed;         356 AA.
AC   Q97II1;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Butyrate kinase 2;
DE            Short=BK 2;
DE            EC=2.7.2.7;
DE   AltName: Full=BKII;
GN   Name=buk2; OrderedLocusNames=CA_C1660;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=10937485;
RA   Huang K.X., Huang S., Rudolph F.B., Bennett G.N.;
RT   "Identification and characterization of a second butyrate kinase from
RT   Clostridium acetobutylicum ATCC 824.";
RL   J. Mol. Microbiol. Biotechnol. 2:33-38(2000).
CC   -!- FUNCTION: Catalyzes the conversion of butyryl-CoA through butyryl
CC       phosphate to butyrate.
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   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000305}.
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DR   EMBL; AE001437; AAK79626.1; -; Genomic_DNA.
DR   PIR; G97104; G97104.
DR   RefSeq; NP_348286.1; NC_003030.1.
DR   RefSeq; WP_010964967.1; NC_003030.1.
DR   AlphaFoldDB; Q97II1; -.
DR   SMR; Q97II1; -.
DR   STRING; 272562.CA_C1660; -.
DR   PRIDE; Q97II1; -.
DR   EnsemblBacteria; AAK79626; AAK79626; CA_C1660.
DR   GeneID; 44998155; -.
DR   KEGG; cac:CA_C1660; -.
DR   PATRIC; fig|272562.8.peg.1863; -.
DR   eggNOG; COG3426; Bacteria.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; CNSNDAR; -.
DR   OrthoDB; 537106at2; -.
DR   BRENDA; 2.7.2.7; 1452.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000000814; 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:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..356
FT                   /note="Butyrate kinase 2"
FT                   /id="PRO_0000107658"
SQ   SEQUENCE   356 AA;  38695 MW;  3D7690A16EE3026B CRC64;
     MKFKLLTINP GSTSTKIAVF ENEKEILSET LRHSSKELEA YKNIYEQFEF RKDTILKVLK
     DKNFNIQNID AVVGRGGLLK PIVGGTYKVN EKMLKDLKAG VQGEHASNLG GIIANSIAEA
     FGVSAYIVDP VVVDEMEDIA RFSGIPELPR KSIFHALNQK AVAKRYAKES ERDYEDLNII
     VAHMGGGVSV GAHKNGKIID VNNALDGEGA FSPERSGNLP SGDLVRLCFS GKYTEDEILK
     KITGKGGFVA YHGTNNALDV QNAALEGDYD AKMTYNAMGY QVAKDIGSAA AVLDGKVDCI
     ILTGGIAYNK LMTDFIAKKV SFIAPITIYP GEDEMLALAE GTLRVLSGQE EAKKYK