DEVR_MYCTO
ID DEVR_MYCTO Reviewed; 217 AA.
AC P9WMF8; L0TBX9; P95193; Q79CX8; Q7D625;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=DNA-binding transcriptional activator DevR/DosR {ECO:0000305};
GN Name=devR; Synonyms=dosR; OrderedLocusNames=MT3219;
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).
RN [2]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
CC -!- FUNCTION: Member of the two-component regulatory system DevR/DevS
CC (DosR/DosS) involved in onset of the dormancy response. Regulates an
CC approximately 48-member regulon (PubMed:12953092). When phosphorylated
CC binds and activates the promoter of DevR regulon genes in response to
CC hypoxia (By similarity). Accepts a phosphate group from DevS (DosS) and
CC from DosT (By similarity). Does not regulate transcription of dosT (By
CC similarity). {ECO:0000250|UniProtKB:P9WMF9,
CC ECO:0000269|PubMed:12953092}.
CC -!- SUBUNIT: Homodimer. Interacts with NarL.
CC {ECO:0000250|UniProtKB:P9WMF9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WMF9}. Host
CC cytoplasmic vesicle, host phagosome {ECO:0000250|UniProtKB:P9WMF9}.
CC -!- INDUCTION: A member of the dormancy regulon. Moderately expressed under
CC aerobic conditions, it is strongly induced in response to reduced
CC oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC {ECO:0000269|PubMed:12953092}.
CC -!- PTM: Phosphorylated on Asp-54 by both DevS (DosS) and DosT.
CC Phosphorylated on Thr-198 and Thr-205 by PknH. Phosphorylation by PknH
CC enhances DevR dimerization. Aspartate phosphorylation and threonine
CC phosphorylation cooperatively enhance DevR binding to DNA (By
CC similarity). {ECO:0000250|UniProtKB:P9WMF9}.
CC -!- MISCELLANEOUS: The dev nomenclature derives from the increased
CC expression (differentially expressed in virulent strain, dev) of these
CC genes in virulent H37Rv versus avirulent H37Ra. The dos nomenclature
CC derives from experiments in M.bovis showing the same genes are
CC essential for dormancy survival. {ECO:0000305}.
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DR EMBL; AE000516; AAK47557.1; -; Genomic_DNA.
DR PIR; F70645; F70645.
DR RefSeq; WP_003416369.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMF8; -.
DR SMR; P9WMF8; -.
DR EnsemblBacteria; AAK47557; AAK47557; MT3219.
DR GeneID; 45427119; -.
DR KEGG; mtc:MT3219; -.
DR PATRIC; fig|83331.31.peg.3469; -.
DR HOGENOM; CLU_000445_90_10_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd06170; LuxR_C_like; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Host cytoplasmic vesicle;
KW Phosphoprotein; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..217
FT /note="DNA-binding transcriptional activator DevR/DosR"
FT /id="PRO_0000427311"
FT DOMAIN 3..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 143..208
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 167..186
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 198
FT /note="Phosphothreonine; by PknH"
FT /evidence="ECO:0000250|UniProtKB:P9WMF9"
FT MOD_RES 205
FT /note="Phosphothreonine; by PknH"
FT /evidence="ECO:0000250|UniProtKB:P9WMF9"
SQ SEQUENCE 217 AA; 23294 MW; 1BA535C26CC4EB51 CRC64;
MVKVFLVDDH EVVRRGLVDL LGADPELDVV GEAGSVAEAM ARVPAARPDV AVLDVRLPDG
NGIELCRDLL SRMPDLRCLI LTSYTSDEAM LDAILAGASG YVVKDIKGME LARAVKDVGA
GRSLLDNRAA AALMAKLRGA AEKQDPLSGL TDQERTLLGL LSEGLTNKQI ADRMFLAEKT
VKNYVSRLLA KLGMERRTQA AVFATELKRS RPPGDGP
