ID   ACER_ACIBT              Reviewed;         297 AA.
AC   P0DUU5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   25-MAY-2022, entry version 3.
DE   RecName: Full=HTH-type transcriptional regulator AceR {ECO:0000305};
GN   Name=aceR {ECO:0000303|PubMed:29481596}; OrderedLocusNames=A1S_2064;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
RN   [2]
RP   FUNCTION, DNA-BINDING, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=29481596; DOI=10.1093/jac/dky034;
RA   Liu Q., Hassan K.A., Ashwood H.E., Gamage H.K.A.H., Li L., Mabbutt B.C.,
RA   Paulsen I.T.;
RT   "Regulation of the aceI multidrug efflux pump gene in Acinetobacter
RT   baumannii.";
RL   J. Antimicrob. Chemother. 73:1492-1500(2018).
RN   [3]
RP   FUNCTION, DNA-BINDING, SUBUNIT, AND DOMAIN.
RX   PubMed=32636271; DOI=10.1073/pnas.2003271117;
RA   Bolla J.R., Howes A.C., Fiorentino F., Robinson C.V.;
RT   "Assembly and regulation of the chlorhexidine-specific efflux pump AceI.";
RL   Proc. Natl. Acad. Sci. U.S.A. 117:17011-17018(2020).
CC   -!- FUNCTION: Regulates the expression of the AceI transporter
CC       (PubMed:29481596). Binds DNA and chlorhexidine (PubMed:29481596,
CC       PubMed:32636271). Binds to regulatory sites within the intergenic
CC       region between the aceI and aceR genes, and affects the interaction
CC       between RNA polymerase (RNAP) and promoter DNA both in the presence and
CC       in the absence of chlorhexidine (PubMed:29481596, PubMed:32636271). In
CC       the absence of chlorhexidine, prevents transcription of the aceI gene
CC       by disrupting interactions between the promoter DNA and RNAP
CC       (PubMed:32636271). In the presence of chlorhexidine, activates
CC       expression of aceI (PubMed:29481596, PubMed:32636271). When AceR
CC       interacts with chlorhexidine, it undergoes a conformational change and
CC       the tetrameric form either releases the DNA or shifts the position of
CC       the DNA-binding region to allow RNAP to bind onto the promoter DNA to
CC       proceed with aceI transcription (PubMed:32636271).
CC       {ECO:0000269|PubMed:29481596, ECO:0000269|PubMed:32636271}.
CC   -!- SUBUNIT: Homodimer and homotetramer (PubMed:32636271). Binding of
CC       chlorhexidine at the inducer-binding domain causes a quaternary
CC       structural change that favors interactions between dimers to form
CC       tetramers (PubMed:32636271). {ECO:0000269|PubMed:32636271}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: Binds DNA via its N-terminal domain and the inducer molecule
CC       via the C-terminal domain. {ECO:0000269|PubMed:32636271}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant shows a decrease in chlorhexidine
CC       resistance. {ECO:0000269|PubMed:29481596}.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000521; ABO12491.2; -; Genomic_DNA.
DR   RefSeq; WP_001024733.1; NZ_CP053098.1.
DR   SMR; P0DUU5; -.
DR   KEGG; acb:A1S_2064; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..297
FT                   /note="HTH-type transcriptional regulator AceR"
FT                   /id="PRO_0000453614"
FT   DOMAIN          1..60
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        20..39
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
SQ   SEQUENCE   297 AA;  34130 MW;  4E4BE95F932FD3DB CRC64;
     MNINQEQLLM FQAVMETGSF SAAARKLGKV PSAVSMSIAN LEIDLNLTLF ERKGREPTPT
     AEARVLYEKT AQLLIEMNQW KQHAHALSTG LEPNLTIVVV SELLHTNWTD YVCLLESRFP
     DLQINIVSAP QEDALQMLLD GSAQLALMFE REHLDNREQF VELKREALIP VISKTHPLAS
     QEHVSYEQIL GTRQIVVASR DETLKPELLF SKHYWRTDNH HSACLMILRN LGWGVLPQEM
     FKENPELNNK LKALDVFDFT PRFEYYVDLV WSRESELGAA ARFLIDYIRN KRMQPAP