ID   ETHR_MYCS2              Reviewed;         217 AA.
AC   A0R666; I7GGF8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=HTH-type transcriptional regulator EthR;
GN   Name=ethR; OrderedLocusNames=MSMEG_6441, MSMEI_6273;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION AS A REPRESSOR ETHA.
RX   PubMed=10869356; DOI=10.1074/jbc.m003744200;
RA   Baulard A.R., Betts J.C., Engohang-Ndong J., Quan S., McAdam R.A.,
RA   Brennan P.J., Locht C., Besra G.S.;
RT   "Activation of the pro-drug ethionamide is regulated in mycobacteria.";
RL   J. Biol. Chem. 275:28326-28331(2000).
CC   -!- FUNCTION: Involved in the repression of teh monooxygenase EthA which is
CC       responsible of the formation of the active metabolite of ethionamide
CC       (ETH). {ECO:0000305|PubMed:10869356}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; CP000480; ABK70466.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42699.1; -; Genomic_DNA.
DR   RefSeq; WP_011731283.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890654.1; NC_008596.1.
DR   AlphaFoldDB; A0R666; -.
DR   SMR; A0R666; -.
DR   STRING; 246196.MSMEI_6273; -.
DR   BindingDB; A0R666; -.
DR   ChEMBL; CHEMBL2163179; -.
DR   EnsemblBacteria; ABK70466; ABK70466; MSMEG_6441.
DR   EnsemblBacteria; AFP42699; AFP42699; MSMEI_6273.
DR   GeneID; 66737717; -.
DR   KEGG; msg:MSMEI_6273; -.
DR   KEGG; msm:MSMEG_6441; -.
DR   PATRIC; fig|246196.19.peg.6266; -.
DR   eggNOG; COG1309; Bacteria.
DR   OMA; TLAHIWV; -.
DR   OrthoDB; 1437290at2; -.
DR   PRO; PR:A0R666; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR   Pfam; PF00440; TetR_N; 1.
DR   PRINTS; PR00455; HTHTETR.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF48498; SSF48498; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..217
FT                   /note="HTH-type transcriptional regulator EthR"
FT                   /id="PRO_0000398580"
FT   DOMAIN          21..81
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT   DNA_BIND        44..63
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            173
FT                   /note="Inhibitor-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            176
FT                   /note="Inhibitor-binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  23512 MW;  37BDD17023464AC5 CRC64;
     MTTASQTRTP RGRRSARPSG DDREAAILAT AQRLLETKKF AEISVDDLAK GAGISRPTFY
     FYFPSKEAVL LSLIDPLIKR ADSGFDNAVE SMPADPQRAI RRGIEIFFNS FGSHPATARA
     GTEALKSSPE FKEFWSGLMQ KWIAATAALI TAERERGAAP DTIPALDLAT SLNLMNERTM
     MAALADEQPG VAPEKVVATL THIWLNSIYG TLPVGTA