QACR_STAAM
ID QACR_STAAM Reviewed; 188 AA.
AC P0A0N3; P23217;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=HTH-type transcriptional regulator QacR;
GN Name=qacR; OrderedLocusNames=SAVP031;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OG Plasmid VRSAp.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699; PLASMID=VRSAp;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; AP003367; BAB47539.1; -; Genomic_DNA.
DR RefSeq; WP_001807342.1; NC_002774.1.
DR PDB; 3BQZ; X-ray; 2.17 A; A/B=1-188.
DR PDB; 3BR0; X-ray; 2.42 A; A/B=1-188.
DR PDB; 3BR1; X-ray; 3.31 A; A/B/D/E=1-188.
DR PDB; 3BR2; X-ray; 2.90 A; A/B/D/E=1-188.
DR PDB; 3BR3; X-ray; 2.80 A; A/B=1-188.
DR PDB; 3BR5; X-ray; 2.90 A; A/B/D/E=1-188.
DR PDB; 3BR6; X-ray; 3.20 A; A/B/D/E=1-188.
DR PDB; 3BT9; X-ray; 2.75 A; A/B/D/E=1-188.
DR PDB; 3BTC; X-ray; 2.90 A; A/B/D/E=1-188.
DR PDB; 3BTI; X-ray; 2.85 A; A/B/D/E=1-188.
DR PDB; 3BTJ; X-ray; 2.98 A; A/B/D/E=1-188.
DR PDB; 3BTL; X-ray; 2.90 A; A/B/D/E=1-188.
DR PDB; 3PM1; X-ray; 2.80 A; A/B=1-188.
DR PDBsum; 3BQZ; -.
DR PDBsum; 3BR0; -.
DR PDBsum; 3BR1; -.
DR PDBsum; 3BR2; -.
DR PDBsum; 3BR3; -.
DR PDBsum; 3BR5; -.
DR PDBsum; 3BR6; -.
DR PDBsum; 3BT9; -.
DR PDBsum; 3BTC; -.
DR PDBsum; 3BTI; -.
DR PDBsum; 3BTJ; -.
DR PDBsum; 3BTL; -.
DR PDBsum; 3PM1; -.
DR AlphaFoldDB; P0A0N3; -.
DR SMR; P0A0N3; -.
DR World-2DPAGE; 0002:P0A0N3; -.
DR PaxDb; P0A0N3; -.
DR EnsemblBacteria; BAB47539; BAB47539; BAB47539.
DR KEGG; sav:SAVP031; -.
DR HOGENOM; CLU_069356_12_2_9; -.
DR OMA; SKGGIYW; -.
DR EvolutionaryTrace; P0A0N3; -.
DR PRO; PR:P0A0N3; -.
DR Proteomes; UP000002481; Plasmid VRSAp.
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_0000070608"
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 TURN 2..4
FT /evidence="ECO:0007829|PDB:3PM1"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:3BQZ"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:3BQZ"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:3BQZ"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3BQZ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3BR3"
FT HELIX 46..68
FT /evidence="ECO:0007829|PDB:3BQZ"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3BQZ"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:3BQZ"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3BQZ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3BQZ"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:3BQZ"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:3BR0"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3BT9"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3BT9"
FT HELIX 117..136
FT /evidence="ECO:0007829|PDB:3BQZ"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:3BQZ"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3BQZ"
FT HELIX 168..184
FT /evidence="ECO:0007829|PDB:3BQZ"
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
