ID   ANOR_ACINO              Reviewed;         238 AA.
AC   A0A0N8YGA2; A0A0A7XVJ1;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Transcriptional activator protein AnoR {ECO:0000305};
GN   Name=anoR {ECO:0000303|PubMed:25975610};
GN   ORFNames=RR32_17455 {ECO:0000312|EMBL:AJB49804.1};
OS   Acinetobacter nosocomialis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=106654;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6411;
RA   McCorrison J., Sanka R., Adams M., Brinkac L., Sutton G., Bonomo R.,
RA   Rojas L.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 17903;
RX   PubMed=25975610; DOI=10.4014/jmb.1504.04069;
RA   Oh M.H., Choi C.H.;
RT   "Role of LuxIR homologue AnoIR in Acinetobacter nosocomialis and the effect
RT   of virstatin on the expression of anoR gene.";
RL   J. Microbiol. Biotechnol. 25:1390-1400(2015).
CC   -!- FUNCTION: Positively regulates the expression of anoI. Required for
CC       biofilm formation and motility. Probably part of a quorum-sensing
CC       system with AnoI.
CC   -!- INDUCTION: Expression is decreased by virstatin.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant exhibits deficiency in biofilm
CC       formation and motility.
CC   -!- SIMILARITY: Belongs to the autoinducer-regulated transcriptional
CC       regulatory protein family. {ECO:0000305}.
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DR   EMBL; CP010368; AJB49804.1; -; Genomic_DNA.
DR   RefSeq; WP_004711094.1; NZ_VLUI01000023.1.
DR   AlphaFoldDB; A0A0N8YGA2; -.
DR   SMR; A0A0N8YGA2; -.
DR   STRING; 106654.B7L44_20120; -.
DR   GeneID; 60877594; -.
DR   KEGG; ano:RR32_17455; -.
DR   PATRIC; fig|106654.21.peg.3482; -.
DR   eggNOG; COG2197; Bacteria.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.450.80; -; 1.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR005143; TF_LuxR_autoind-bd_dom.
DR   InterPro; IPR036693; TF_LuxR_autoind-bd_dom_sf.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF03472; Autoind_bind; 1.
DR   Pfam; PF00196; GerE; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF75516; SSF75516; 1.
DR   PROSITE; PS00622; HTH_LUXR_1; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Quorum sensing; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..238
FT                   /note="Transcriptional activator protein AnoR"
FT                   /id="PRO_0000438128"
FT   DOMAIN          170..236
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   DNA_BIND        195..214
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
SQ   SEQUENCE   238 AA;  27328 MW;  72DC121CC7F82768 CRC64;
     MESWQEDLLS AFLVVKNEDE LFEVVKSTAS KLGFDYCAYG MQSPLSIAEP KTIMLNNYPQ
     AWQKRYIEQR YVKVDPTVQH CMVSLQPLVW SSQNAKTQEE KDFWEEARSY GLNVGWAQSS
     RDFIGTRGML TLARSTDQLS EKEQKAQYTN MYWLTQTVHS SIAKIVNDVE FSQFNLYLTN
     REKEALRWTA EGKTSAEIAQ IIGVTERTVN FHLCNSMQKL NVNNKISAAI RAVMLGLL