ID   Q8KLP4_STEMA            Unreviewed;       219 AA.
AC   Q8KLP4;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Repressor {ECO:0000313|EMBL:CAC87048.1};
GN   Name=smeT {ECO:0000313|EMBL:CAC87048.1};
OS   Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS   maltophilia).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=40324 {ECO:0000313|EMBL:CAC87048.1};
RN   [1] {ECO:0000313|EMBL:CAC87048.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D457R {ECO:0000313|EMBL:CAC87048.1};
RX   PubMed=12384340; DOI=10.1128/AAC.46.11.3386-3393.2002;
RA   Sanchez P., Alonso A., Martinez J.L.;
RT   "Cloning and characterization of SmeT, a repressor of the Stenotrophomonas
RT   maltophilia multidrug efflux pump SmeDEF.";
RL   Antimicrob. Agents Chemother. 46:3386-3393(2002).
RN   [2] {ECO:0007829|PDB:2W53}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RX   PubMed=19324881; DOI=10.1074/jbc.M809221200;
RA   Hernandez A., Mate M.J., Sanchez-Diaz P.C., Romero A., Rojo F.,
RA   Martinez J.L.;
RT   "Structural and functional analysis of SmeT, the repressor of the
RT   Stenotrophomonas maltophilia multidrug efflux pump SmeDEF.";
RL   J. Biol. Chem. 284:14428-14438(2009).
RN   [3] {ECO:0007829|PDB:3P9T}
RP   X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS).
RX   PubMed=21738470; DOI=10.1371/journal.ppat.1002103;
RA   Hernandez A., Ruiz F.M., Romero A., Martinez J.L.;
RT   "The binding of triclosan to SmeT, the repressor of the multidrug efflux
RT   pump SmeDEF, induces antibiotic resistance in Stenotrophomonas
RT   maltophilia.";
RL   PLoS Pathog. 7:e1002103-e1002103(2011).
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DR   EMBL; AJ316010; CAC87048.1; -; Genomic_DNA.
DR   PDB; 2W53; X-ray; 2.00 A; A/B=1-219.
DR   PDB; 3P9T; X-ray; 2.02 A; A/B=1-219.
DR   PDBsum; 2W53; -.
DR   PDBsum; 3P9T; -.
DR   AlphaFoldDB; Q8KLP4; -.
DR   SMR; Q8KLP4; -.
DR   EvolutionaryTrace; Q8KLP4; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR   InterPro; IPR013572; Tscrpt_reg_MAATS_C.
DR   PANTHER; PTHR30055:SF148; HTH-TYPE TRANSCRIPTIONAL REGULATOR ACRR; 1.
DR   PANTHER; PTHR30055; HTH-TYPE TRANSCRIPTIONAL REGULATOR RUTR; 1.
DR   Pfam; PF08361; TetR_C_2; 1.
DR   Pfam; PF00440; TetR_N; 1.
DR   PRINTS; PR00455; HTHTETR.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF48498; Tetracyclin repressor-like, C-terminal domain; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2W53, ECO:0007829|PDB:3P9T};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00335}.
FT   DOMAIN          10..70
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50977"
FT   DNA_BIND        33..52
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00335"
SQ   SEQUENCE   219 AA;  24623 MW;  AE640E4085815BE8 CRC64;
     MARKTKEDTQ ATREGILDAA EACFHEHGVA RTTLEMIGAR AGYTRGAVYW HFKNKSEVLA
     AIVERVHLPF MQELERTSTD QRDTPVHDLR AVMIHSFIEL SEDERLRKTM EIMLRSDASA
     NTRVLTEMQQ AGFRDALDRM ERALRRARDL GQLREGADPK IAARMQHATV LGVLHGAMVE
     PELMDLKRDG MLALDMTLAA YVKDGVFVPG TVPEPLPEA
//