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