ACUA_BACLD
ID ACUA_BACLD Reviewed; 210 AA.
AC Q65G33; Q62RI8;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Acetoin utilization protein AcuA {ECO:0000312|EMBL:AAU41981.1};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P39065, ECO:0000312|EMBL:AAU41981.1};
DE AltName: Full=Acetoin dehydrogenase {ECO:0000312|EMBL:AAU24622.1};
DE AltName: Full=Protein acetyltransferase AcuA {ECO:0000250|UniProtKB:P39065};
GN Name=acuA {ECO:0000312|EMBL:AAU41981.1};
GN OrderedLocusNames=BL00376, BLi03120;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1] {ECO:0000312|EMBL:AAU41981.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46 {ECO:0000312|EMBL:AAU41981.1};
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2] {ECO:0000312|EMBL:AAU24622.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
RN [3] {ECO:0000305}
RP INDUCTION BY GLUCOSE STARVATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46 {ECO:0000269|PubMed:17274076};
RX PubMed=17274076; DOI=10.1002/pmic.200600556;
RA Voigt B., Hoi le T., Jurgen B., Albrecht D., Ehrenreich A., Veith B.,
RA Evers S., Maurer K.H., Hecker M., Schweder T.;
RT "The glucose and nitrogen starvation response of Bacillus licheniformis.";
RL Proteomics 7:413-423(2007).
RN [4] {ECO:0000305}
RP OPERON STRUCTURE, INDUCTION BY GLUCOSE STARVATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46 {ECO:0000269|PubMed:20524112};
RX PubMed=20524112; DOI=10.1007/s00253-010-2681-5;
RA Thanh T.N., Jurgen B., Bauch M., Liebeke M., Lalk M., Ehrenreich A.,
RA Evers S., Maurer K.H., Antelmann H., Ernst F., Homuth G., Hecker M.,
RA Schweder T.;
RT "Regulation of acetoin and 2,3-butanediol utilization in Bacillus
RT licheniformis.";
RL Appl. Microbiol. Biotechnol. 87:2227-2235(2010).
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:0000250|UniProtKB:P39065, ECO:0000269|PubMed:20524112}.
CC -!- PATHWAY: Ketone degradation; acetoin degradation.
CC {ECO:0000250|UniProtKB:P39065}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P39065}.
CC -!- INDUCTION: Induced by glucose starvation conditions.
CC {ECO:0000269|PubMed:17274076, ECO:0000269|PubMed:20524112}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype on growth in medium
CC containing glucose and acetoin or in medium with acetate compared to
CC wild-type. After glucose exhaustion acetoin is quickly consumed
CC similarly to wild-type. In the late exponential growth phase slightly
CC more pyruvate is produced compared to wild-type.
CC {ECO:0000269|PubMed:20524112}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000255}.
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DR EMBL; AE017333; AAU41981.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU24622.1; -; Genomic_DNA.
DR RefSeq; WP_003184432.1; NC_006322.1.
DR AlphaFoldDB; Q65G33; -.
DR SMR; Q65G33; -.
DR STRING; 279010.BL00376; -.
DR EnsemblBacteria; AAU24622; AAU24622; BL00376.
DR GeneID; 66214906; -.
DR KEGG; bld:BLi03120; -.
DR KEGG; bli:BL00376; -.
DR eggNOG; COG0454; Bacteria.
DR HOGENOM; CLU_113703_0_0_9; -.
DR OMA; KIMEKMM; -.
DR OrthoDB; 1812368at2; -.
DR BioCyc; BLIC279010:BLI_RS15425-MON; -.
DR UniPathway; UPA00040; -.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0019152; F:acetoin dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0043894; F:acetyl-CoA synthetase acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0045150; P:acetoin catabolic process; IMP:UniProtKB.
DR GO; GO:0034078; P:butanediol catabolic process; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:UniProtKB.
DR GO; GO:0031669; P:cellular response to nutrient levels; IMP:UniProtKB.
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; Transferase.
FT CHAIN 1..210
FT /note="Acetoin utilization protein AcuA"
FT /id="PRO_0000422612"
FT DOMAIN 19..189
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 210 AA; 24555 MW; 5B1CE5FA1742CE7F CRC64;
MEHHKTYHAK ELQTEKGSVL IEGPISPEKL AEYEFHDELT AFRPSQKQHE ALIEIAGLPE
GRIIIARFRQ TIVGYVTYVY PDPLERWSEG NMENLIELGA IEVIPAFRGH SVGKTLLAVS
MMDPQMEKYI IITTEYYWHW DLKGTNKDVW EYRKMMEKMM NAGGLVWFAT DDPEISSHPA
NCLMARIGKE VSQESIERFD RLRFHNRFMY
