ID   CTFB_CLOAB              Reviewed;         221 AA.
AC   P23673;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Acetoacetyl-CoA:acetate/butyrate CoA-transferase beta subunit {ECO:0000305};
DE            EC=2.8.3.9 {ECO:0000269|PubMed:2383002, ECO:0000269|PubMed:2719476};
DE   AltName: Full=Butyrate--acetoacetate CoA-transferase subunit B {ECO:0000303|PubMed:2383002};
DE            Short=Coat B;
GN   Name=ctfB {ECO:0000303|PubMed:8226639}; OrderedLocusNames=CA_P0164;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OG   Plasmid pSOL1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=2254264; DOI=10.1128/jb.172.12.6907-6918.1990;
RA   Gerischer U., Duerre P.;
RT   "Cloning, sequencing, and molecular analysis of the acetoacetate
RT   decarboxylase gene region from Clostridium acetobutylicum.";
RL   J. Bacteriol. 172:6907-6918(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=8226639; DOI=10.1128/jb.175.21.6959-6969.1993;
RA   Fischer R.J., Helms J., Duerre P.;
RT   "Cloning, sequencing, and molecular analysis of the sol operon of
RT   Clostridium acetobutylicum, a chromosomal locus involved in
RT   solventogenesis.";
RL   J. Bacteriol. 175:6959-6969(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19.
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=8423010; DOI=10.1016/0378-1119(93)90545-e;
RA   Petersen D.J., Cary J.W., Vanderleyden J., Bennett G.N.;
RT   "Sequence and arrangement of genes encoding enzymes of the acetone-
RT   production pathway of Clostridium acetobutylicum ATCC824.";
RL   Gene 123:93-97(1993).
RN   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 1-8, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=2383002; DOI=10.1128/aem.56.6.1576-1583.1990;
RA   Cary J.W., Petersen D.J., Papoutsakis E.T., Bennett G.N.;
RT   "Cloning and expression of Clostridium acetobutylicum ATCC 824 acetoacetyl-
RT   coenzyme A:acetate/butyrate:coenzyme A-transferase in Escherichia coli.";
RL   Appl. Environ. Microbiol. 56:1576-1583(1990).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=2719476; DOI=10.1128/aem.55.2.323-329.1989;
RA   Wiesenborn D.P., Rudolph F.B., Papoutsakis E.T.;
RT   "Coenzyme A transferase from Clostridium acetobutylicum ATCC 824 and its
RT   role in the uptake of acids.";
RL   Appl. Environ. Microbiol. 55:323-329(1989).
CC   -!- FUNCTION: Catalyzes the transfer of CoA from acetoacetyl-CoA to
CC       acetate, butyrate and propionate (PubMed:2719476, PubMed:2383002).
CC       Shows also low activity with valerate, isobutyrate and crotonate
CC       (PubMed:2719476). Plays an important role in the metabolic shift
CC       between the acid-producing and solvent-forming states of
CC       C.acetobutylicum (PubMed:2383002). Acts mainly to detoxify the medium
CC       by removing the acetate and butyrate excreted earlier in the
CC       fermentation (PubMed:2719476, PubMed:2383002).
CC       {ECO:0000269|PubMed:2383002, ECO:0000269|PubMed:2719476,
CC       ECO:0000303|PubMed:2383002, ECO:0000303|PubMed:2719476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetoacetate + butanoyl-CoA = acetoacetyl-CoA + butanoate;
CC         Xref=Rhea:RHEA:12961, ChEBI:CHEBI:13705, ChEBI:CHEBI:17968,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57371; EC=2.8.3.9;
CC         Evidence={ECO:0000269|PubMed:2383002, ECO:0000269|PubMed:2719476};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12963;
CC         Evidence={ECO:0000269|PubMed:2719476};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetoacetate + acetyl-CoA = acetate + acetoacetyl-CoA;
CC         Xref=Rhea:RHEA:27806, ChEBI:CHEBI:13705, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57288;
CC         Evidence={ECO:0000269|PubMed:2383002, ECO:0000269|PubMed:2719476};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27808;
CC         Evidence={ECO:0000269|PubMed:2719476};
CC   -!- ACTIVITY REGULATION: The acetate and butyrate conversion reactions are
CC       inhibited in vitro by physiological levels of acetone and butanol.
CC       {ECO:0000269|PubMed:2719476}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1200 mM for acetate {ECO:0000269|PubMed:2719476};
CC         KM=660 mM for butyrate {ECO:0000269|PubMed:2719476};
CC         KM=1000 mM for propionate {ECO:0000269|PubMed:2719476};
CC         KM=0.021 mM for acetoacetyl-CoA (in the presence of acetate)
CC         {ECO:0000269|PubMed:2719476};
CC         KM=0.056 mM for acetoacetyl-CoA (in the presence of butyrate)
CC         {ECO:0000269|PubMed:2719476};
CC         KM=0.007 mM for acetoacetyl-CoA (in the presence of propionate)
CC         {ECO:0000269|PubMed:2719476};
CC       pH dependence:
CC         Shows at least 80% of maximal activity from pH 5.9 to greater than
CC         7.8 for acetate conversion. {ECO:0000269|PubMed:2719476};
CC   -!- SUBUNIT: Heterotetramer composed of two alpha subunits (CtfA) and two
CC       beta subunits (CtfB). {ECO:0000269|PubMed:2719476}.
CC   -!- INDUCTION: Transcriptionally induced or derepressed before the onset of
CC       solventogenesis. {ECO:0000269|PubMed:8226639}.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; M55392; AAA63762.1; -; Genomic_DNA.
DR   EMBL; X72831; CAA51346.1; -; Genomic_DNA.
DR   EMBL; M93363; AAB53233.1; -; Genomic_DNA.
DR   EMBL; AE001438; AAK76909.1; -; Genomic_DNA.
DR   PIR; JN0489; JN0489.
DR   RefSeq; NP_149327.1; NC_001988.2.
DR   RefSeq; WP_010890848.1; NC_001988.2.
DR   AlphaFoldDB; P23673; -.
DR   SMR; P23673; -.
DR   GeneID; 45000389; -.
DR   KEGG; cac:CA_P0164; -.
DR   PATRIC; fig|272562.8.peg.165; -.
DR   HOGENOM; CLU_019942_4_1_9; -.
DR   OrthoDB; 9778604at2; -.
DR   BioCyc; MetaCyc:COATBCLOS-MONOMER; -.
DR   SABIO-RK; P23673; -.
DR   Proteomes; UP000000814; Plasmid pSOL1.
DR   GO; GO:0047371; F:butyrate-acetoacetate CoA-transferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR004164; CoA_transf_AS.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02428; pcaJ_scoB_fam; 1.
DR   PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1.
DR   PANTHER; PTHR13707:SF23; SUCCINYL-COA:3-KETOACID-COENZYME A TRANSFERASE; 1.
DR   Pfam; PF01144; CoA_trans; 1.
DR   SMART; SM00882; CoA_trans; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR   PROSITE; PS01274; COA_TRANSF_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Plasmid; Reference proteome; Transferase.
FT   CHAIN           1..221
FT                   /note="Acetoacetyl-CoA:acetate/butyrate CoA-transferase
FT                   beta subunit"
FT                   /id="PRO_0000157926"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
SQ   SEQUENCE   221 AA;  23624 MW;  9F9920709628F800 CRC64;
     MINDKNLAKE IIAKRVAREL KNGQLVNLGV GLPTMVADYI PKNFKITFQS ENGIVGMGAS
     PKINEADKDV VNAGGDYTTV LPDGTFFDSS VSFSLIRGGH VDVTVLGALQ VDEKGNIANW
     IVPGKMLSGM GGAMDLVNGA KKVIIAMRHT NKGQPKILKK CTLPLTAKSQ ANLIVTELGV
     IEVINDGLLL TEINKNTTID EIRSLTAADL LISNELRPMA V
//