QACR_STAAU
ID QACR_STAAU Reviewed; 188 AA.
AC P0A0N4; D2JG66; P23217;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=HTH-type transcriptional regulator QacR;
GN Name=qacR; ORFNames=SAP100B_005, SAP104C_022;
OS Staphylococcus aureus.
OG Plasmid pSK1, Plasmid SAP104C, and Plasmid pSK17.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK18; PLASMID=pSK1;
RX PubMed=2089219; DOI=10.1111/j.1365-2958.1990.tb00565.x;
RA Rouch D.A., Cram D.S., Diberardino D., Littlejohn T.G., Skurray R.A.;
RT "Efflux-mediated antiseptic resistance gene qacA from Staphylococcus
RT aureus: common ancestry with tetracycline- and sugar-transport proteins.";
RL Mol. Microbiol. 4:2051-2062(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK6575, and SK707; PLASMID=pSK17, and SAP104C;
RA Gill J., Borman J., Shetty J., Hostetler J., Durkin S., Montgomery B.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK6575, and SK707; PLASMID=pSK17, and SAP104C;
RA Summers A.O., Shearer J., Wireman J.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK18; PLASMID=pSK1;
RX PubMed=20547176; DOI=10.1016/j.plasmid.2010.06.001;
RA Jensen S.O., Apisiridej S., Kwong S.M., Yang Y.H., Skurray R.A., Firth N.;
RT "Analysis of the prototypical Staphylococcus aureus multiresistance plasmid
RT pSK1.";
RL Plasmid 64:135-142(2010).
RN [5]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF N-TERMINUS.
RC STRAIN=SK982; PLASMID=pSK1;
RX PubMed=9660841; DOI=10.1074/jbc.273.29.18665;
RA Grkovic S., Brown M.H., Roberts N.J., Paulsen I.T., Skurray R.A.;
RT "QacR is a repressor protein that regulates expression of the
RT Staphylococcus aureus multidrug efflux pump QacA.";
RL J. Biol. Chem. 273:18665-18673(1998).
RN [6]
RP MUTAGENESIS OF CYS-72 AND CYS-141.
RX PubMed=11717268; DOI=10.1128/jb.183.24.7102-7109.2001;
RA Grkovic S., Brown M.H., Schumacher M.A., Brennan R.G., Skurray R.A.;
RT "The staphylococcal QacR multidrug regulator binds a correctly spaced
RT operator as a pair of dimers.";
RL J. Bacteriol. 183:7102-7109(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS).
RX PubMed=11739955; DOI=10.1126/science.1066020;
RA Schumacher M.A., Miller M.C., Grkovic S., Brown M.H., Skurray R.A.,
RA Brennan R.G.;
RT "Structural mechanisms of QacR induction and multidrug recognition.";
RL Science 294:2158-2163(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=11867549; DOI=10.1093/emboj/21.5.1210;
RA Schumacher M.A., Miller M.C., Grkovic S., Brown M.H., Skurray R.A.,
RA Brennan R.G.;
RT "Structural basis for cooperative DNA binding by two dimers of the
RT multidrug-binding protein QacR.";
RL EMBO J. 21:1210-1218(2002).
RN [9]
RP ERRATUM OF PUBMED:11867549.
RA Schumacher M.A., Miller M.C., Grkovic S., Brown M.H., Skurray R.A.,
RA Brennan R.G.;
RL EMBO J. 21:2301-2301(2002).
RN [10]
RP REVIEW.
RX PubMed=12648720; DOI=10.1016/s0923-2508(02)00013-x;
RA Schumacher M.A., Brennan R.G.;
RT "Deciphering the molecular basis of multidrug recognition: crystal
RT structures of the Staphylococcus aureus multidrug binding transcription
RT regulator QacR.";
RL Res. Microbiol. 154:69-77(2003).
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.
CC -!- SUBUNIT: Homodimer. Binds cooperatively to DNA as a pair of dimers.
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DR EMBL; GQ900498; ADA80841.1; -; Genomic_DNA.
DR EMBL; GQ900514; ADA80909.1; -; Genomic_DNA.
DR EMBL; GU565967; ADK23698.1; -; Genomic_DNA.
DR PIR; S12393; S12393.
DR RefSeq; WP_001807342.1; NZ_WBTO01000037.1.
DR RefSeq; YP_003813122.1; NC_014369.1.
DR PDB; 1JT0; X-ray; 2.90 A; A/B/C/D=1-188.
DR PDB; 1JT6; X-ray; 2.54 A; A/B/D/E=1-188.
DR PDB; 1JTX; X-ray; 2.85 A; A/B/D/E=1-188.
DR PDB; 1JTY; X-ray; 2.97 A; A/B/D/E=1-188.
DR PDB; 1JUM; X-ray; 2.98 A; A/B/D/E=1-188.
DR PDB; 1JUP; X-ray; 2.95 A; A/B/D/E=1-188.
DR PDB; 1JUS; X-ray; 2.84 A; A/B/D/E=1-188.
DR PDB; 1QVT; X-ray; 2.89 A; A/B/D/E=1-188.
DR PDB; 1QVU; X-ray; 2.96 A; A/B/D/E=1-188.
DR PDB; 1RKW; X-ray; 2.62 A; A/B/D/E=1-188.
DR PDB; 1RPW; X-ray; 2.90 A; A/B/C/D=1-188.
DR PDB; 2DTZ; X-ray; 2.80 A; A/B/D/E=1-188.
DR PDB; 2GBY; X-ray; 2.90 A; A/B/D/E=1-188.
DR PDB; 2HQ5; X-ray; 2.80 A; A/B/D/E=1-188.
DR PDBsum; 1JT0; -.
DR PDBsum; 1JT6; -.
DR PDBsum; 1JTX; -.
DR PDBsum; 1JTY; -.
DR PDBsum; 1JUM; -.
DR PDBsum; 1JUP; -.
DR PDBsum; 1JUS; -.
DR PDBsum; 1QVT; -.
DR PDBsum; 1QVU; -.
DR PDBsum; 1RKW; -.
DR PDBsum; 1RPW; -.
DR PDBsum; 2DTZ; -.
DR PDBsum; 2GBY; -.
DR PDBsum; 2HQ5; -.
DR AlphaFoldDB; P0A0N4; -.
DR SMR; P0A0N4; -.
DR DrugBank; DB04209; Dequalinium.
DR DrugBank; DB03608; Diminazene.
DR DrugBank; DB03808; Hexamidine.
DR DrugBank; DB01123; Proflavine.
DR OMA; SKGGIYW; -.
DR EvolutionaryTrace; P0A0N4; -.
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; Direct protein sequencing; DNA-binding; Plasmid; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..188
FT /note="HTH-type transcriptional regulator QacR"
FT /id="PRO_0000070609"
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 MUTAGEN 72
FT /note="C->A: Almost no loss of activity."
FT /evidence="ECO:0000269|PubMed:11717268"
FT MUTAGEN 141
FT /note="C->A,S: Almost no loss of activity."
FT /evidence="ECO:0000269|PubMed:11717268"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:1JT6"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1JT6"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1JTX"
FT HELIX 46..66
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:1JT6"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:1JT6"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 111..136
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:1JT6"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1JT6"
FT HELIX 168..186
FT /evidence="ECO:0007829|PDB:1JT6"
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
