ACOR_BACSU
ID ACOR_BACSU Reviewed; 605 AA.
AC O31551; O31406; Q79F13;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Acetoin dehydrogenase operon transcriptional activator AcoR;
GN Name=acoR; Synonyms=yfjG, yzcB; OrderedLocusNames=BSU08100;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT region of the Bacillus subtilis chromosome containing genes for trehalose
RT metabolism and acetoin utilization.";
RL Microbiology 142:3057-3065(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-587.
RC STRAIN=168 / ATCC 33234 / DSM 402 / NBRC 111470 / NCIMB 10106;
RX PubMed=10368162; DOI=10.1128/jb.181.12.3837-3841.1999;
RA Huang M., Oppermann-Sanio F.B., Steinbuechel A.;
RT "Biochemical and molecular characterization of the Bacillus subtilis
RT acetoin catabolic pathway.";
RL J. Bacteriol. 181:3837-3841(1999).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=11274109; DOI=10.1128/jb.183.8.2497-2504.2001;
RA Ali N.O., Bignon J., Rapoport G., Debarbouille M.;
RT "Regulation of the acetoin catabolic pathway is controlled by sigma L in
RT Bacillus subtilis.";
RL J. Bacteriol. 183:2497-2504(2001).
RN [5]
RP FUNCTION.
RX PubMed=16944132; DOI=10.1007/s00253-006-0549-5;
RA Silbersack J., Juergen B., Hecker M., Schneidinger B., Schmuck R.,
RA Schweder T.;
RT "An acetoin-regulated expression system of Bacillus subtilis.";
RL Appl. Microbiol. Biotechnol. 73:895-903(2006).
CC -!- FUNCTION: Acts as a transcriptional activator of the acoABCL operon
CC encoding the acetoin dehydrogenase complex.
CC {ECO:0000269|PubMed:11274109, ECO:0000269|PubMed:16944132}.
CC -!- INDUCTION: Negatively controlled by CcpA, a global regulator of carbon
CC catabolite repression. {ECO:0000269|PubMed:11274109}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC05586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D78509; BAA24292.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12639.1; -; Genomic_DNA.
DR EMBL; AF006075; AAC05586.1; ALT_INIT; Genomic_DNA.
DR PIR; H69581; H69581.
DR RefSeq; NP_388691.1; NC_000964.3.
DR RefSeq; WP_003244100.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31551; -.
DR SMR; O31551; -.
DR STRING; 224308.BSU08100; -.
DR PaxDb; O31551; -.
DR PRIDE; O31551; -.
DR DNASU; 936148; -.
DR EnsemblBacteria; CAB12639; CAB12639; BSU_08100.
DR GeneID; 936148; -.
DR KEGG; bsu:BSU08100; -.
DR PATRIC; fig|224308.179.peg.876; -.
DR eggNOG; COG3284; Bacteria.
DR InParanoid; O31551; -.
DR OMA; HTLGMVK; -.
DR PhylomeDB; O31551; -.
DR BioCyc; BSUB:BSU08100-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 2: Evidence at transcript level;
KW Activator; ATP-binding; DNA-binding; Nucleotide-binding;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..605
FT /note="Acetoin dehydrogenase operon transcriptional
FT activator AcoR"
FT /id="PRO_0000361683"
FT DOMAIN 295..520
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 578..597
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 323..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 387..396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT CONFLICT 550
FT /note="P -> A (in Ref. 3; AAC05586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 67160 MW; 59B594470E9CD8CC CRC64;
MNSVPNDLQT WKRFVKDGVL DEARLRKRIA ESWHRCKKAE VNPYLEKGPK VLQQTELDQQ
SKKHSFFLTT AKPYLEKLLP AIKEMEMMAL LIDSDGVVLA LDGHPRALYE AKRINFVEGA
CWTETAVGTN AIGTALHISE PVAIQGSEHY SIASHLWNCS AAPIHHEDGS LAGVIDISCP
AAGAHPHMLG IATAIAYAAE RELAAKSREK ELELISRFGE RAASSVPMVL CNTKQHIISA
SMPIRTSMPD WQGRHLYELK ERGYSIENAV TIGDGGTCFY LSEQKKKKAF RFNGVIGQSG
RSQAMLMHLE RAAATDASVC LSGETGTGKE VAARALHENS ERRHGPFVAV NCGAIPSDLI
ESELFGYAEG AFTGAKRNGY KGAFQKANQG TLFLDEIGEI SHSMQVALLR VLQERKITPI
GGTKEIPVDI RVIAATHCDL RELAENGKIR EDLFYRLHVY PIELPPLRDR TEDIPDLFEY
YKQKNHWPGD LPSDFCNVLK QWKWPGNIRE LFNVFERLSI RFPDGRLRDE SLPALLEAAG
LPASSAEKKP AAAGVLTFRE QIQKDMMIKA LESAKGNVSQ AAKISGIPRS TFYKRLKKFN
LSAES
