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Database: UniProt
Entry: A0A1P8YMW3_9NOCA
LinkDB: A0A1P8YMW3_9NOCA
Original site: A0A1P8YMW3_9NOCA 
ID   A0A1P8YMW3_9NOCA        Unreviewed;       205 AA.
AC   A0A1P8YMW3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Bacterial regulatory, tetR family protein {ECO:0000313|EMBL:AQA25255.1};
GN   ORFNames=BTZ20_1663 {ECO:0000313|EMBL:AQA25255.1};
OS   Rhodococcus sp. MTM3W5.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1805827 {ECO:0000313|EMBL:AQA25255.1, ECO:0000313|Proteomes:UP000187995};
RN   [1] {ECO:0000313|EMBL:AQA25255.1, ECO:0000313|Proteomes:UP000187995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTM3W5.2 {ECO:0000313|EMBL:AQA25255.1,
RC   ECO:0000313|Proteomes:UP000187995};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; CP019572; AQA25255.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1P8YMW3; -.
DR   STRING; 1805827.BTZ20_1663; -.
DR   Proteomes; UP000187995; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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   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   Pfam; PF02909; TetR_C_1; 1.
DR   Pfam; PF00440; TetR_N; 1.
DR   PRINTS; PR00400; TETREPRESSOR.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF48498; Tetracyclin repressor-like, C-terminal domain; 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   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1..55
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50977"
FT   DNA_BIND        18..37
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00335"
SQ   SEQUENCE   205 AA;  22141 MW;  8E5D0BAE7722AB5E CRC64;
     MLRAAVAYAD EHGIASLSMR KLGEALAVEA MSLYNHVANK DDLLDGMVDH VFGEIVMDPG
     ASGWRQAMRL RAISAREVLS RHRWAIGLLD SRSSPGPATL RHHDAVLGSL RAGGFSVPMA
     AHAFAVLDSY IYGFALQEAA LPFEGPQETE DLAQAILEGM PADEFPHLTE LAVEHVLQPG
     YEFGSEFEFG LDLILDGLER ASVAG
//
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