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Database: UniProt
Entry: A0A1I0G227_9ACTN
LinkDB: A0A1I0G227_9ACTN
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ID   A0A1I0G227_9ACTN        Unreviewed;       313 AA.
AC   A0A1I0G227;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Regulatory protein, tetR family {ECO:0000313|EMBL:SET64736.1};
GN   ORFNames=SAMN05421811_103713 {ECO:0000313|EMBL:SET64736.1};
OS   Nonomuraea wenchangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=568860 {ECO:0000313|EMBL:SET64736.1, ECO:0000313|Proteomes:UP000199361};
RN   [1] {ECO:0000313|EMBL:SET64736.1, ECO:0000313|Proteomes:UP000199361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5598 {ECO:0000313|EMBL:SET64736.1,
RC   ECO:0000313|Proteomes:UP000199361};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: TetR is the repressor of the tetracycline resistance element;
CC       its N-terminal region forms a helix-turn-helix structure and binds DNA.
CC       Binding of tetracycline to TetR reduces the repressor affinity for the
CC       tetracycline resistance gene (tetA) promoter operator sites.
CC       {ECO:0000256|ARBA:ARBA00002856}.
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DR   EMBL; FOHX01000003; SET64736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0G227; -.
DR   STRING; 568860.SAMN05421811_103713; -.
DR   OrthoDB; 4540879at2; -.
DR   Proteomes; UP000199361; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR004111; Repressor_TetR_C.
DR   InterPro; IPR003012; Tet_transcr_reg_TetR.
DR   InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR46577; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR   PANTHER; PTHR46577:SF1; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR   Pfam; PF00392; GntR; 1.
DR   Pfam; PF02909; TetR_C_1; 1.
DR   Pfam; PF00440; TetR_N; 1.
DR   PRINTS; PR00400; TETREPRESSOR.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF48498; Tetracyclin repressor-like, C-terminal domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   4: Predicted;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00335};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199361}.
FT   DOMAIN          3..71
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
FT   DOMAIN          94..154
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50977"
FT   DNA_BIND        117..136
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00335"
FT   REGION          72..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  34168 MW;  AF7E9AF20A15ECD3 CRC64;
     MDTPPYARIA GDIKRRIADG RLRPGDRVPS TRQLARDWDV ALATAAKALA LLAQEGVVIA
     EPRVGTVVAE QRGPGRPAAR RGAGQAARGP GRPGDARERV VRAAVELADA DGLDELTMRA
     LADRLGMATM SLYRHVSGKD ELVLLMVDAV IDDHPLPEER PAGWRETLET SARLQWAAYR
     AHPWMAGVTS LYRPLPSAGL LKHSEWVMSA LAGTRLDATA KMNVHILLYS FVQGLAANFE
     QERRARAATG LSDEEWMSAQ EERMRAVSES PGYGAFAAFL GELGEFDLDL DRLFEFGLRP
     LLDGLARQID QPG
//
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