ID   HTHR_STRCO              Reviewed;         192 AA.
AC   Q9ADP7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=HTH-type transcriptional repressor SCO4008;
GN   OrderedLocusNames=SCO4008;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, DNA-BINDING, ACTIVITY
RP   REGULATION, SUBUNIT, INDUCTION, AND DOMAIN.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=23831227; DOI=10.1016/j.jmb.2013.06.013;
RA   Hayashi T., Tanaka Y., Sakai N., Okada U., Yao M., Watanabe N., Tamura T.,
RA   Tanaka I.;
RT   "SCO4008, a putative TetR transcriptional repressor from Streptomyces
RT   coelicolor A3(2), regulates transcription of sco4007 by multidrug
RT   recognition.";
RL   J. Mol. Biol. 425:3289-3300(2013).
CC   -!- FUNCTION: Probably regulates the expression of its own gene and the
CC       adjacent SCO4007 gene by binding to two operator sites in the SCO4007-
CC       SCO4008 intergenic region. {ECO:0000269|PubMed:23831227}.
CC   -!- ACTIVITY REGULATION: Binding of a wide range of cationic hydrophobic
CC       compounds to SCO4008 causes a decrease in DNA-binding, probably via
CC       allosteric conformational change of SCO4008.
CC       {ECO:0000269|PubMed:23831227}.
CC   -!- SUBUNIT: Homodimer. Four dimers bind to the two operator sites.
CC       {ECO:0000269|PubMed:23831227}.
CC   -!- INDUCTION: Autoregulated. {ECO:0000305|PubMed:23831227}.
CC   -!- DOMAIN: Contains an N-terminal DNA-binding domain and a C-terminal
CC       dimerization domain. {ECO:0000269|PubMed:23831227}.
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DR   EMBL; AL939118; CAC32348.1; -; Genomic_DNA.
DR   RefSeq; NP_628190.1; NC_003888.3.
DR   RefSeq; WP_011029378.1; NZ_VNID01000032.1.
DR   PDB; 2D6Y; X-ray; 2.30 A; A/B=1-192.
DR   PDBsum; 2D6Y; -.
DR   AlphaFoldDB; Q9ADP7; -.
DR   SMR; Q9ADP7; -.
DR   STRING; 100226.SCO4008; -.
DR   GeneID; 1099444; -.
DR   KEGG; sco:SCO4008; -.
DR   PATRIC; fig|100226.15.peg.4071; -.
DR   eggNOG; COG1309; Bacteria.
DR   HOGENOM; CLU_069356_1_2_11; -.
DR   InParanoid; Q9ADP7; -.
DR   OMA; RLLFWEG; -.
DR   PhylomeDB; Q9ADP7; -.
DR   EvolutionaryTrace; Q9ADP7; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR041467; Sco4008_C.
DR   InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR   Pfam; PF17926; TetR_C_21; 1.
DR   Pfam; PF00440; TetR_N; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF48498; SSF48498; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..192
FT                   /note="HTH-type transcriptional repressor SCO4008"
FT                   /id="PRO_0000426730"
FT   DOMAIN          7..67
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT   DNA_BIND        30..49
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..24
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   TURN            25..27
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           31..38
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           42..49
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           52..70
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           78..91
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           94..106
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           114..133
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           143..159
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           161..168
FT                   /evidence="ECO:0007829|PDB:2D6Y"
FT   HELIX           171..190
FT                   /evidence="ECO:0007829|PDB:2D6Y"
SQ   SEQUENCE   192 AA;  21272 MW;  93AA98FA74CA1E87 CRC64;
     MAARDPEATK ARIFEAAVAE FARHGIAGAR IDRIAAEARA NKQLIYAYYG NKGELFASVL
     EKKMLDLAIS VPVDPDDIEG WIDRLLDYHA AHPELLRLLF WEGMEYGTAE LPHEAERQEH
     YARKVAAVRD GQERGVITDA IPAPDLLFLL VAMANWAVVV PQMKRILVGG GDAGTDGLRD
     SIKKAARRIV DR