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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//