ACUA_BACSU
ID ACUA_BACSU Reviewed; 210 AA.
AC P39065;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Acetoin utilization protein AcuA;
DE EC=2.3.1.-;
DE AltName: Full=Protein acetyltransferase AcuA;
GN Name=acuA; OrderedLocusNames=BSU29690;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, OPERON STRUCTURE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=7934817; DOI=10.1111/j.1365-2958.1993.tb01952.x;
RA Grundy F.J., Waters D.A., Takova T.Y., Henkin T.M.;
RT "Identification of genes involved in utilization of acetate and acetoin in
RT Bacillus subtilis.";
RL Mol. Microbiol. 10:259-271(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION BY GLUCOSE AND CCPA.
RX PubMed=7913927; DOI=10.1128/jb.176.15.4527-4533.1994;
RA Grundy F.J., Turinsky A.J., Henkin T.M.;
RT "Catabolite regulation of Bacillus subtilis acetate and acetoin utilization
RT genes by CcpA.";
RL J. Bacteriol. 176:4527-4533(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / SMY;
RX PubMed=16855235; DOI=10.1128/jb.00215-06;
RA Gardner J.G., Grundy F.J., Henkin T.M., Escalante-Semerena J.C.;
RT "Control of acetyl-coenzyme A synthetase (AcsA) activity by
RT acetylation/deacetylation without NAD(+) involvement in Bacillus
RT subtilis.";
RL J. Bacteriol. 188:5460-5468(2006).
RN [6]
RP INDUCTION.
RX PubMed=17322312; DOI=10.1128/jb.01736-06;
RA Keijser B.J., Ter Beek A., Rauwerda H., Schuren F., Montijn R.,
RA van der Spek H., Brul S.;
RT "Analysis of temporal gene expression during Bacillus subtilis spore
RT germination and outgrowth.";
RL J. Bacteriol. 189:3624-3634(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ARG-43; THR-170; HIS-178 AND
RP GLY-188.
RX PubMed=18487328; DOI=10.1128/jb.00340-08;
RA Gardner J.G., Escalante-Semerena J.C.;
RT "Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme
RT that controls the activity of the acetyl coenzyme a synthetase (AcsA) in
RT Bacillus subtilis.";
RL J. Bacteriol. 190:5132-5136(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / SMY;
RX PubMed=19136592; DOI=10.1128/jb.01674-08;
RA Gardner J.G., Escalante-Semerena J.C.;
RT "In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN
RT gene (formerly yhdZ), and functions encoded by the acuABC genes control the
RT activity of acetyl coenzyme A synthetase.";
RL J. Bacteriol. 191:1749-1755(2009).
CC -!- FUNCTION: Part of the acuABC operon, which is possibly involved in the
CC breakdown of acetoin and butanediol. Acts as an acetyltransferase
CC inactivating acetyl-CoA synthetase AcsA via acetylation at a Lys
CC residue. {ECO:0000269|PubMed:16855235, ECO:0000269|PubMed:18487328,
CC ECO:0000269|PubMed:19136592, ECO:0000269|PubMed:7934817}.
CC -!- ACTIVITY REGULATION: Activity is sensitive to salt concentration, a
CC high concentration of KCL (500 mM) is needed for complete inactivation.
CC {ECO:0000269|PubMed:18487328}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 mM for acetyl-CoA {ECO:0000269|PubMed:16855235,
CC ECO:0000269|PubMed:18487328};
CC Vmax=0.8 mmol/min/mg enzyme {ECO:0000269|PubMed:16855235,
CC ECO:0000269|PubMed:18487328};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:16855235,
CC ECO:0000269|PubMed:18487328};
CC Temperature dependence:
CC Optimum temperature 37 degrees Celsius. Thermostable. Retains 93, 78
CC and 15 % of its protein acetyltransferase activity after heating to
CC 100 degrees Celsius for 5, 30 and 60 minutes, respectively.
CC {ECO:0000269|PubMed:16855235, ECO:0000269|PubMed:18487328};
CC -!- PATHWAY: Ketone degradation; acetoin degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18487328}.
CC -!- INDUCTION: Expression is maximal in stationary phase and is repressed
CC by the addition of glucose to the growth medium. CcpA protein is
CC required for glucose repression. Acetoin does not act as an inducer.
CC Up-regulated during the 80 to 100 minutes of spore germination and into
CC the outgrowth phase. {ECO:0000269|PubMed:17322312,
CC ECO:0000269|PubMed:7913927}.
CC -!- DISRUPTION PHENOTYPE: Does not impair growth on acetate. Disruption
CC together with other acetoin utilization genes acuB and acuC results in
CC poor growth and sporulation on acetoin or butanediol. Triple deletion
CC of acuA, acuC and srtN improves the growth on acetate but it does not
CC reach that of wild-type under low-acetate conditions.
CC {ECO:0000269|PubMed:16855235, ECO:0000269|PubMed:19136592,
CC ECO:0000269|PubMed:7934817}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; L17309; AAA68286.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00396.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14947.1; -; Genomic_DNA.
DR PIR; S39645; S39645.
DR RefSeq; NP_390847.1; NC_000964.3.
DR RefSeq; WP_003229296.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39065; -.
DR SMR; P39065; -.
DR STRING; 224308.BSU29690; -.
DR PaxDb; P39065; -.
DR PRIDE; P39065; -.
DR EnsemblBacteria; CAB14947; CAB14947; BSU_29690.
DR GeneID; 937633; -.
DR KEGG; bsu:BSU29690; -.
DR PATRIC; fig|224308.179.peg.3227; -.
DR eggNOG; COG0454; Bacteria.
DR OMA; KIMEKMM; -.
DR PhylomeDB; P39065; -.
DR BioCyc; BSUB:BSU29690-MON; -.
DR BRENDA; 2.3.1.B34; 658.
DR SABIO-RK; P39065; -.
DR UniPathway; UPA00040; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0019152; F:acetoin dehydrogenase activity; IGI:UniProtKB.
DR GO; GO:0043894; F:acetyl-CoA synthetase acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0045150; P:acetoin catabolic process; IGI:UniProtKB.
DR GO; GO:0034078; P:butanediol catabolic process; IGI:UniProtKB.
DR GO; GO:0045014; P:carbon catabolite repression of transcription by glucose; IDA:UniProtKB.
DR GO; GO:0071311; P:cellular response to acetate; IGI:UniProtKB.
DR GO; GO:0009847; P:spore germination; IEP:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR024699; AcuA.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR PIRSF; PIRSF021278; AcuA; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetoin catabolism; Acyltransferase; Reference proteome; Sporulation;
KW Transferase.
FT CHAIN 1..210
FT /note="Acetoin utilization protein AcuA"
FT /id="PRO_0000074571"
FT DOMAIN 20..161
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT MUTAGEN 43
FT /note="R->H: 25% retention of activity. Two to three-fold
FT reduction in KM for acetyl-CoA. Three-fold slower turnover
FT number. Retains 54% of the activity of the wild-type after
FT heating it to 100 degrees Celsius for 30 minutes."
FT /evidence="ECO:0000269|PubMed:18487328"
FT MUTAGEN 170
FT /note="T->A: 25% retention of activity. Two to three fold
FT reduction in KM for acetyl-CoA. Three-fold slower turnover
FT number. Retains 60% of the activity of the wild-type after
FT heating it to 100 degrees Celsius for 30 minutes."
FT /evidence="ECO:0000269|PubMed:18487328"
FT MUTAGEN 178
FT /note="H->P: Inactive. Leads to a rapid turnover of the
FT enzyme."
FT /evidence="ECO:0000269|PubMed:18487328"
FT MUTAGEN 188
FT /note="G->E: Inactive. Leads to a rapid turnover of the
FT enzyme."
FT /evidence="ECO:0000269|PubMed:18487328"
SQ SEQUENCE 210 AA; 24333 MW; 74DB94A46E8556DA CRC64;
MEHHKTYHSA NIKTATGSLL IEGPVSPEDL AGYEFHKDLT AFRPPREQHE ALVDIAGLPE
GRIIIARDGR TIVGYVTYLY PDPLERWSEG NMEDLIELGA IEVAPDYRGC AVGKTLLTVS
MMDEQMENYI VMTTEYYWHW DLKGMKKDVW EYRKIMEKMM NAGGLVWFAT DEPEISSHPA
NCLMARIGKN VSQESIEQFD RLRFYHRYMY
