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QACR_STAHA
ID   QACR_STAHA              Reviewed;         188 AA.
AC   P0A0N5; P23217;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=HTH-type transcriptional regulator QacR;
GN   Name=qacR;
OS   Staphylococcus haemolyticus.
OG   Plasmid pNVH97A.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NVH97A; PLASMID=pNVH97A;
RX   PubMed=12384372; DOI=10.1128/aac.46.11.3606-3612.2002;
RA   Anthonisen I.-L., Sunde M., Steinum T.M., Sidhu M.S., Sorum H.;
RT   "Organization of the antiseptic resistance gene qacA and Tn552-related
RT   beta-lactamase genes in multidrug-resistant Staphylococcus haemolyticus
RT   strains of animal and human origins.";
RL   Antimicrob. Agents Chemother. 46:3606-3612(2002).
CC   -!- FUNCTION: Transcriptional repressor of qacA. Binds to IR1, an unusually
CC       long 28 bp operator, which is located downstream from the qacA promoter
CC       and overlaps its transcription start site. QacR is induced from its IR1
CC       site by binding to one of many structurally dissimilar cationic
CC       lipophilic compounds, which are also substrates of QacA (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Binds cooperatively to DNA as a pair of dimers (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; AJ400722; CAB94807.1; -; Genomic_DNA.
DR   RefSeq; WP_001807342.1; NZ_LOSE02000002.1.
DR   PDB; 2G0E; X-ray; 2.88 A; A/B/D/E=1-188.
DR   PDBsum; 2G0E; -.
DR   AlphaFoldDB; P0A0N5; -.
DR   SMR; P0A0N5; -.
DR   DrugBank; DB04115; Berberine.
DR   DrugBank; DB03808; Hexamidine.
DR   DrugBank; DB03895; Malachite Green.
DR   DrugBank; DB03825; Rhodamine 6G.
DR   EvolutionaryTrace; P0A0N5; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR   InterPro; IPR013571; Tscrpt_reg_QacR_C.
DR   Pfam; PF08360; TetR_C_5; 1.
DR   Pfam; PF00440; TetR_N; 1.
DR   PRINTS; PR00455; HTHTETR.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF48498; SSF48498; 1.
DR   PROSITE; PS01081; HTH_TETR_1; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Plasmid; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..188
FT                   /note="HTH-type transcriptional regulator QacR"
FT                   /id="PRO_0000070610"
FT   DOMAIN          1..61
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT   DNA_BIND        24..43
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           25..30
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           46..66
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           75..88
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           96..105
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   TURN            110..117
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           118..136
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           145..161
FT                   /evidence="ECO:0007829|PDB:2G0E"
FT   HELIX           168..186
FT                   /evidence="ECO:0007829|PDB:2G0E"
SQ   SEQUENCE   188 AA;  22174 MW;  7B91E005C8D47322 CRC64;
     MNLKDKILGV AKELFIKNGY NATTTGEIVK LSESSKGNLY YHFKTKENLF LEILNIEESK
     WQEQWKKEQI KCKTNREKFY LYNELSLTTE YYYPLQNAII EFYTEYYKTN SINEKMNKLE
     NKYIDAYHVI FKEGNLNGEW CINDVNAVSK IAANAVNGIV TFTHEQNINE RIKLMNKFSQ
     IFLNGLSK
 
 
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