ID   ACOR_CUPNH              Reviewed;         668 AA.
AC   P28614; Q0K4X6;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Acetoin catabolism regulatory protein;
GN   Name=acoR; OrderedLocusNames=H16_B0142;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX   PubMed=1378052; DOI=10.1128/jb.174.13.4391-4400.1992;
RA   Krueger N., Steinbuechel A.;
RT   "Identification of acoR, a regulatory gene for the expression of genes
RT   essential for acetoin catabolism in Alcaligenes eutrophus H16.";
RL   J. Bacteriol. 174:4391-4400(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- FUNCTION: Required for sigma-54-dependent transcription of acoXABC.
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DR   EMBL; M90471; AAA21944.1; -; Genomic_DNA.
DR   EMBL; AM260480; CAJ94948.1; -; Genomic_DNA.
DR   PIR; A42890; A42890.
DR   RefSeq; WP_011616377.1; NZ_CP039288.1.
DR   AlphaFoldDB; P28614; -.
DR   SMR; P28614; -.
DR   STRING; 381666.H16_B0142; -.
DR   EnsemblBacteria; CAJ94948; CAJ94948; H16_B0142.
DR   GeneID; 57646021; -.
DR   KEGG; reh:H16_B0142; -.
DR   eggNOG; COG3284; Bacteria.
DR   HOGENOM; CLU_000445_8_12_4; -.
DR   OMA; HFRAAFI; -.
DR   OrthoDB; 123059at2; -.
DR   Proteomes; UP000008210; Chromosome 2.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:UniProtKB-KW.
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; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
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; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   1: Evidence at protein level;
KW   Acetoin catabolism; Activator; ATP-binding; Direct protein sequencing;
KW   DNA-binding; Nucleotide-binding; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..668
FT                   /note="Acetoin catabolism regulatory protein"
FT                   /id="PRO_0000081318"
FT   DOMAIN          341..570
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        630..649
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          586..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..609
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         369..376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         433..442
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   CONFLICT        211
FT                   /note="E -> Q (in Ref. 1; AAA21944)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   668 AA;  72962 MW;  7244EF079EDA9F24 CRC64;
     MDLRQREHIE TVVQATTYLA PPAVLADRIA HDAIIQNSWR RCVHQYGLDP SRMQEARILP
     QPRLREHQER IDDFARIARH GLQSLYGQVA GLGYVVLLTD AQGVTVDYIG EARSDAALRH
     AGLYLGAEWS ESGAGTCAVG TALATGQALT VHQADHFDAT HIPLTCTAAP LFDTHGNLHA
     ILDISALTSP QAKDSQGLAL QMVRIYAAHI ENANFLRAHR RDWILKLNVA PEFVDVNPEY
     LLALDEAGRI VGHNHRARLM LEGELGGAPG ATVLGQRFET LFDARLEDLG HYVYSRPSEQ
     RLVALTRSGG LLYLSVLPPA LRWQAPPAET QVAMPDALAA LTGGDAALQL QLQRAARLVD
     SPINLLIHGE TGSGKEFLAK ALHLASARRG GPFVAVNCAA IPETLIESEL FGHLPNSFSG
     AGPRGKRGLI QEADGGTLFL DEIGDMPREL QSRLLRVLAE GEVLPVGAAR PVPVRLRVIS
     ATHHSLEQLV ADGRFREDLY YRLNGARFTL PPLRARTDLD WLVRKLLQEG SAEGSEITLS
     PAARERLHRH RWPGNLRELR NVLEYARAVC ADGYIDVPDL PDSLAGPAPS AALPQPGPAQ
     SPAAAPFDPH QLPPEGMLLM QYLRASGWNL SAVARQIGVS RMTLYRRMER YGIQSPNRRD
     GGPEPTDA