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Database: UniProt
Entry: Q9XCC7_STRFR
LinkDB: Q9XCC7_STRFR
Original site: Q9XCC7_STRFR 
ID   Q9XCC7_STRFR            Unreviewed;       226 AA.
AC   Q9XCC7;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=Gamma-butyrolactone receptor protein TylP {ECO:0000313|EMBL:AAD40801.1};
GN   Name=tylP {ECO:0000313|EMBL:AAD40801.1};
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1906 {ECO:0000313|EMBL:AAD40801.1};
RN   [1] {ECO:0000313|EMBL:AAD40801.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T59235 {ECO:0000313|EMBL:AAD40801.1};
RX   PubMed=10467127; DOI=10.1016/S1074-5521(99)80113-6;
RA   Bate N., Butler A.R., Gandecha A.R., Cundliffe E.;
RT   "Multiple regulatory genes in the tylosin biosynthetic cluster of
RT   Streptomyces fradiae.";
RL   Chem. Biol. 6:617-624(1999).
RN   [2] {ECO:0007829|PDB:5XAY, ECO:0007829|PDB:5XAZ}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-226.
RX   PubMed=28739805; DOI=10.1074/jbc.M117.788000;
RA   Ray S., Maitra A., Biswas A., Panjikar S., Mondal J., Anand R.;
RT   "Functional insights into the mode of DNA and ligand binding of the TetR
RT   family regulator TylP from <i>Streptomyces fradiae</i>.";
RL   J. Biol. Chem. 292:15301-15311(2017).
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DR   EMBL; AF145049; AAD40801.1; -; Genomic_DNA.
DR   PIR; T44586; T44586.
DR   RefSeq; WP_043470766.1; NZ_MCNU01000172.1.
DR   PDB; 5XAY; X-ray; 2.58 A; A/B/C/D/E/F/G/H=2-226.
DR   PDB; 5XAZ; X-ray; 2.30 A; A/B/C/D/E/F/G/H=2-226.
DR   PDBsum; 5XAY; -.
DR   PDBsum; 5XAZ; -.
DR   AlphaFoldDB; Q9XCC7; -.
DR   SMR; Q9XCC7; -.
DR   PATRIC; fig|1906.11.peg.6051; -.
DR   eggNOG; COG1309; Bacteria.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
DR   Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1.
DR   InterPro; IPR047923; ArpA-like.
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   NCBIfam; NF041196; ScbR_bind_reg; 1.
DR   PANTHER; PTHR47506:SF3; HTH-TYPE TRANSCRIPTIONAL REGULATOR LMRA; 1.
DR   PANTHER; PTHR47506; TRANSCRIPTIONAL REGULATORY PROTEIN; 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; PS01081; HTH_TETR_1; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5XAY, ECO:0007829|PDB:5XAZ};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00335};
KW   Receptor {ECO:0000313|EMBL:AAD40801.1};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          8..68
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50977"
FT   DNA_BIND        31..50
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00335"
SQ   SEQUENCE   226 AA;  24820 MW;  863175B923E26DF4 CRC64;
     MARQERAAQT RRTIVAAAAA VFDELGYEAT TIAEILKRSG VTKGALYFHF TSKEQLAQEV
     LTSQLRAVPP VEEQRLVLQQ IIDETLLLAQ LLSKGDPLVR GSVRLTVEPG APRDGLDRRA
     PMQEWIGHGR DLLRRAEAGG ELLPRLDVDA VARMLVGGFT GAQILSNILT GHADLLERVT
     DMHRHLMTSV AVPAVLVRLD FSAERSITVY DEAMRRREAP LPAAGD
//
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