ETHR_MYCTO
ID ETHR_MYCTO Reviewed; 216 AA.
AC P9WMC0; L0TDZ6; P96222; Q7D4Q7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=HTH-type transcriptional regulator EthR;
GN Name=ethR; Synonyms=etaR; OrderedLocusNames=MT3970;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Involved in the repression of the monooxygenase EthA which is
CC responsible of the formation of the active metabolite of ethionamide
CC (ETH). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AE000516; AAK48337.1; -; Genomic_DNA.
DR PIR; D70655; D70655.
DR RefSeq; WP_003399797.1; NZ_KK341227.1.
DR PDB; 4M3F; X-ray; 2.00 A; A=1-216.
DR PDBsum; 4M3F; -.
DR AlphaFoldDB; P9WMC0; -.
DR SMR; P9WMC0; -.
DR EnsemblBacteria; AAK48337; AAK48337; MT3970.
DR GeneID; 45427859; -.
DR KEGG; mtc:MT3970; -.
DR PATRIC; fig|83331.31.peg.4269; -.
DR HOGENOM; CLU_069356_32_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProt.
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 3D-structure; DNA-binding; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..216
FT /note="HTH-type transcriptional regulator EthR"
FT /id="PRO_0000427330"
FT DOMAIN 23..83
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 46..65
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 68..92
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 132..158
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 168..187
FT /evidence="ECO:0007829|PDB:4M3F"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:4M3F"
SQ SEQUENCE 216 AA; 23757 MW; 129DEAB3320514B6 CRC64;
MTTSAASQAS LPRGRRTARP SGDDRELAIL ATAENLLEDR PLADISVDDL AKGAGISRPT
FYFYFPSKEA VLLTLLDRVV NQADMALQTL AENPADTDRE NMWRTGINVF FETFGSHKAV
TRAGQAARAT SVEVAELWST FMQKWIAYTA AVIDAERDRG AAPRTLPAHE LATALNLMNE
RTLFASFAGE QPSVPEARVL DTLVHIWVTS IYGENR
