DEVR_MYCTU
ID DEVR_MYCTU Reviewed; 217 AA.
AC P9WMF9; L0TBX9; P95193; Q79CX8; Q7D625;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=DNA-binding transcriptional activator DevR/DosR {ECO:0000305};
GN Name=devR {ECO:0000303|PubMed:10970762}; Synonyms=dosR;
GN OrderedLocusNames=Rv3133c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION (MICROBIAL
RP INFECTION), AND OPERON STRUCTURE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=10970762; DOI=10.1054/tuld.2000.0240;
RA Dasgupta N., Kapur V., Singh K.K., Das T.K., Sachdeva S., Jyothisri K.,
RA Tyagi J.S.;
RT "Characterization of a two-component system, devR-devS, of Mycobacterium
RT tuberculosis.";
RL Tuber. Lung Dis. 80:141-159(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP FUNCTION, REGULON, INDUCTION BY HYPOXIA, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11416222; DOI=10.1073/pnas.121172498;
RA Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA Schoolnik G.K.;
RT "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT encoding alpha -crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
RN [4]
RP DISRUPTION PHENOTYPE IN DBA/2 MICE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12595424; DOI=10.1128/iai.71.3.1134-1140.2003;
RA Parish T., Smith D.A., Kendall S., Casali N., Bancroft G.J., Stoker N.G.;
RT "Deletion of two-component regulatory systems increases the virulence of
RT Mycobacterium tuberculosis.";
RL Infect. Immun. 71:1134-1140(2003).
RN [5]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
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).
RN [6]
RP DNA-BINDING, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-54.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=12694625; DOI=10.1046/j.1365-2958.2003.03474.x;
RA Park H.D., Guinn K.M., Harrell M.I., Liao R., Voskuil M.I., Tompa M.,
RA Schoolnik G.K., Sherman D.R.;
RT "Rv3133c/dosR is a transcription factor that mediates the hypoxic response
RT of Mycobacterium tuberculosis.";
RL Mol. Microbiol. 48:833-843(2003).
RN [7]
RP FUNCTION, PHOSPHORYLATION AT ASP-54 BY DEVS (DOSS), PHOSPHORYLATION BY
RP DOST, AND REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15033981; DOI=10.1074/jbc.m401230200;
RA Roberts D.M., Liao R.P., Wisedchaisri G., Hol W.G., Sherman D.R.;
RT "Two sensor kinases contribute to the hypoxic response of Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 279:23082-23087(2004).
RN [8]
RP PHOSPHORYLATION AT ASP-54 BY DEVS (DOSS), AND MUTAGENESIS OF ASP-8; ASP-9;
RP ASP-54 AND LYS-104.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15073296; DOI=10.1099/mic.0.26218-0;
RA Saini D.K., Malhotra V., Dey D., Pant N., Das T.K., Tyagi J.S.;
RT "DevR-DevS is a bona fide two-component system of Mycobacterium
RT tuberculosis that is hypoxia-responsive in the absence of the DNA-binding
RT domain of DevR.";
RL Microbiology 150:865-875(2004).
RN [9]
RP INDUCTION BY CARBON MONOXIDE (CO).
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17609369; DOI=10.1073/pnas.0705054104;
RA Kumar A., Toledo J.C., Patel R.P., Lancaster J.R. Jr., Steyn A.J.;
RT "Mycobacterium tuberculosis DosS is a redox sensor and DosT is a hypoxia
RT sensor.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11568-11573(2007).
RN [10]
RP INDUCTION BY CARBON MONOXIDE (CO), AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA Shiloh M.U., Manzanillo P., Cox J.S.;
RT "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT macrophage infection.";
RL Cell Host Microbe 3:323-330(2008).
RN [11]
RP FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, AND DNA-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18359816; DOI=10.1128/jb.01308-07;
RA Chauhan S., Tyagi J.S.;
RT "Cooperative binding of phosphorylated DevR to upstream sites is necessary
RT and sufficient for activation of the Rv3134c-devRS operon in Mycobacterium
RT tuberculosis: implication in the induction of DevR target genes.";
RL J. Bacteriol. 190:4301-4312(2008).
RN [12]
RP INDUCTION BY CARBON MONOXIDE (CO), DISRUPTION PHENOTYPE, AND ROLE IN
RP DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18400743; DOI=10.1074/jbc.m802274200;
RA Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I.,
RA Agarwal A., Steyn A.J.;
RT "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
RT tuberculosis dormancy regulon.";
RL J. Biol. Chem. 283:18032-18039(2008).
RN [13]
RP DISRUPTION PHENOTYPE IN GUINEA PIG; MOUSE AND RABBIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19103767; DOI=10.1128/iai.01117-08;
RA Converse P.J., Karakousis P.C., Klinkenberg L.G., Kesavan A.K., Ly L.H.,
RA Allen S.S., Grosset J.H., Jain S.K., Lamichhane G., Manabe Y.C.,
RA McMurray D.N., Nuermberger E.L., Bishai W.R.;
RT "Role of the dosR-dosS two-component regulatory system in Mycobacterium
RT tuberculosis virulence in three animal models.";
RL Infect. Immun. 77:1230-1237(2009).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=19487478; DOI=10.1128/iai.01449-08;
RA Honaker R.W., Leistikow R.L., Bartek I.L., Voskuil M.I.;
RT "Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium
RT tuberculosis dormancy.";
RL Infect. Immun. 77:3258-3263(2009).
RN [15]
RP PHOSPHORYLATION AT THR-198 AND THR-205 BY PKNH, AND MUTAGENESIS OF THR-198
RP AND THR-205.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20630871; DOI=10.1074/jbc.m110.132894;
RA Chao J.D., Papavinasasundaram K.G., Zheng X., Chavez-Steenbock A., Wang X.,
RA Lee G.Q., Av-Gay Y.;
RT "Convergence of Ser/Thr and two-component signaling to coordinate
RT expression of the dormancy regulon in Mycobacterium tuberculosis.";
RL J. Biol. Chem. 285:29239-29246(2010).
RN [16]
RP FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-82, AND DNA-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21764934; DOI=10.1128/jb.05051-11;
RA Gautam U.S., Sikri K., Tyagi J.S.;
RT "The residue threonine 82 of DevR (DosR) is essential for DevR activation
RT and function in Mycobacterium tuberculosis despite its atypical location.";
RL J. Bacteriol. 193:4849-4858(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [18]
RP INTERACTION WITH NARL.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=25659431; DOI=10.1074/jbc.m114.591800;
RA Malhotra V., Agrawal R., Duncan T.R., Saini D.K., Clark-Curtiss J.E.;
RT "Mycobacterium tuberculosis response regulators, DevR and NarL, interact in
RT vivo and co-regulate gene expression during aerobic nitrate metabolism.";
RL J. Biol. Chem. 290:8294-8309(2015).
RN [19]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=28977726; DOI=10.1111/febs.14284;
RA Sousa E.H.S., Gonzalez G., Gilles-Gonzalez M.A.;
RT "Target DNA stabilizes Mycobacterium tuberculosis DevR/DosR phosphorylation
RT by the full-length oxygen sensors DevS/DosS and DosT.";
RL FEBS J. 284:3954-3967(2017).
RN [20]
RP REVIEW.
RX PubMed=25002970; DOI=10.3390/bios3030259;
RA Sivaramakrishnan S., de Montellano P.R.;
RT "The DosS-DosT/DosR mycobacterial sensor system.";
RL Biosensors 3:259-282(2013).
RN [21] {ECO:0007744|PDB:1ZLJ, ECO:0007744|PDB:1ZLK}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-217 WITH AND WITHOUT BOUND
RP DNA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16246368; DOI=10.1016/j.jmb.2005.09.048;
RA Wisedchaisri G., Wu M., Rice A.E., Roberts D.M., Sherman D.R., Hol W.G.;
RT "Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex
RT involved in gene activation during adaptation to hypoxic latency.";
RL J. Mol. Biol. 354:630-641(2005).
RN [22] {ECO:0007744|PDB:3C3W, ECO:0007744|PDB:3C57}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18353359; DOI=10.1016/j.jmb.2008.02.029;
RA Wisedchaisri G., Wu M., Sherman D.R., Hol W.G.;
RT "Crystal structures of the response regulator DosR from Mycobacterium
RT tuberculosis suggest a helix rearrangement mechanism for phosphorylation
RT activation.";
RL J. Mol. Biol. 378:227-242(2008).
CC -!- FUNCTION: Member of the two-component regulatory system DevR/DevS (also
CC called DosR/DosS) involved in onset of the dormancy response
CC (PubMed:15033981). Regulates an approximately 48-member regulon
CC (PubMed:12953092, PubMed:11416222, PubMed:15033981, PubMed:18400743).
CC When phosphorylated binds and activates the promoter of DevR regulon
CC genes in response to hypoxia (PubMed:18359816, PubMed:21764934,
CC PubMed:28977726). The presence of target DNA increases stability of
CC phospho-DevR in vitro (PubMed:28977726). Activates its own
CC transcription under hypoxic but not aerobic conditions, probably binds
CC as a dimer to tandem binding sites within the devR and hspX promoters
CC (PubMed:18359816). Accepts a phosphate group from DevS (DosS) and from
CC DosT (PubMed:15033981, PubMed:15073296, PubMed:21764934,
CC PubMed:28977726). Does not regulate transcription of dosT
CC (PubMed:19487478). {ECO:0000269|PubMed:11416222,
CC ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:15033981,
CC ECO:0000269|PubMed:15073296, ECO:0000269|PubMed:18359816,
CC ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:19487478,
CC ECO:0000269|PubMed:21764934, ECO:0000269|PubMed:28977726}.
CC -!- SUBUNIT: Homodimer (PubMed:18353359). Interacts with NarL
CC (PubMed:25659431). {ECO:0000269|PubMed:18353359,
CC ECO:0000269|PubMed:25659431}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle, host phagosome
CC {ECO:0000269|PubMed:10970762}. Note=(Microbial infection) In human
CC monocytes after in vitro infection (PubMed:10970762).
CC {ECO:0000269|PubMed:10970762}.
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), low levels of nitric oxide (NO) and carbon
CC monoxide (CO) (PubMed:11416222, PubMed:12953092, PubMed:17609369,
CC PubMed:18474359, PubMed:18400743). It is hoped that this regulon will
CC give insight into the latent, or dormant phase of infection. Expression
CC under hypoxic conditions, but not aerobically, is autoregulated. Member
CC of the Rv3134c-devR-devS operon (PubMed:10970762).
CC {ECO:0000269|PubMed:10970762, ECO:0000269|PubMed:11416222,
CC ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:17609369,
CC ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:18474359}.
CC -!- PTM: Phosphorylated on Asp-54 by both DevS (DosS) and DosT
CC (PubMed:15033981, PubMed:15073296, PubMed:21764934). Phosphorylated on
CC Thr-198 and Thr-205 by PknH, which enhances DevR dimerization
CC (PubMed:20630871). Aspartate phosphorylation and threonine
CC phosphorylation cooperatively enhance DevR binding to DNA
CC (PubMed:20630871). {ECO:0000269|PubMed:15033981,
CC ECO:0000269|PubMed:15073296, ECO:0000269|PubMed:20630871,
CC ECO:0000269|PubMed:21764934}.
CC -!- DISRUPTION PHENOTYPE: Strains deleted for this gene show hypervirulence
CC upon intravenous inoculation in the mouse and DBA/2 model
CC (PubMed:12595424). However contradictory results were shown for using a
CC devR/devS deletion strain in rabbits, guinea pigs and C57BL/6 mice
CC (PubMed:19103767). All studies agree that deletion strains fail to
CC induce the dormancy regulon genes in response to hypoxia, NO, and CO
CC (PubMed:11416222, PubMed:12694625, PubMed:18474359, PubMed:18400743,
CC PubMed:19487478). Deletion has no effect on expression of dosT
CC (PubMed:19487478). {ECO:0000269|PubMed:11416222,
CC ECO:0000269|PubMed:12595424, ECO:0000269|PubMed:12694625,
CC ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:18474359,
CC ECO:0000269|PubMed:19103767, ECO:0000269|PubMed:19487478}.
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 (dos). {ECO:0000305|PubMed:25002970}.
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DR EMBL; U22037; AAD17452.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45943.1; -; Genomic_DNA.
DR PIR; F70645; F70645.
DR RefSeq; NP_217649.1; NC_000962.3.
DR RefSeq; WP_003416369.1; NZ_NVQJ01000019.1.
DR PDB; 1ZLJ; X-ray; 2.00 A; A/B/C/D/E/F/G/H=144-217.
DR PDB; 1ZLK; X-ray; 3.10 A; A/B=144-217.
DR PDB; 3C3W; X-ray; 2.20 A; A/B=1-217.
DR PDB; 3C57; X-ray; 1.70 A; A/B=144-217.
DR PDBsum; 1ZLJ; -.
DR PDBsum; 1ZLK; -.
DR PDBsum; 3C3W; -.
DR PDBsum; 3C57; -.
DR AlphaFoldDB; P9WMF9; -.
DR SMR; P9WMF9; -.
DR IntAct; P9WMF9; 1.
DR STRING; 83332.Rv3133c; -.
DR BindingDB; P9WMF9; -.
DR ChEMBL; CHEMBL6064; -.
DR iPTMnet; P9WMF9; -.
DR PaxDb; P9WMF9; -.
DR DNASU; 888842; -.
DR GeneID; 45427119; -.
DR GeneID; 888842; -.
DR KEGG; mtu:Rv3133c; -.
DR TubercuList; Rv3133c; -.
DR eggNOG; COG2197; Bacteria.
DR OMA; DDPMMQL; -.
DR PhylomeDB; P9WMF9; -.
DR PHI-base; PHI:3614; -.
DR PRO; PR:P9WMF9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:MTBBASE.
DR GO; GO:0005615; C:extracellular space; IDA:MTBBASE.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0072493; C:host cell endosome lumen; IDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MTBBASE.
DR GO; GO:0022611; P:dormancy process; IDA:MTBBASE.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IMP:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Host cytoplasmic vesicle;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..217
FT /note="DNA-binding transcriptional activator DevR/DosR"
FT /id="PRO_0000392625"
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 ECO:0000305|PubMed:15033981, ECO:0000305|PubMed:15073296"
FT MOD_RES 198
FT /note="Phosphothreonine; by PknH"
FT /evidence="ECO:0000269|PubMed:20630871"
FT MOD_RES 205
FT /note="Phosphothreonine; by PknH"
FT /evidence="ECO:0000269|PubMed:20630871"
FT MUTAGEN 8
FT /note="D->N: No phosphorylation by DevS (DosS)."
FT /evidence="ECO:0000269|PubMed:15073296"
FT MUTAGEN 9
FT /note="D->N: No phosphorylation by DevS (DosS)."
FT /evidence="ECO:0000269|PubMed:15073296"
FT MUTAGEN 54
FT /note="D->E: Able to bind DNA, no longer induces hypoxic
FT response."
FT /evidence="ECO:0000269|PubMed:12694625,
FT ECO:0000269|PubMed:15073296"
FT MUTAGEN 54
FT /note="D->V: No phosphorylation by DevS (DosS) nor by
FT DosT."
FT /evidence="ECO:0000269|PubMed:12694625,
FT ECO:0000269|PubMed:15073296"
FT MUTAGEN 82
FT /note="T->A: No longer induces expression of DevR regulon
FT under hypoxic conditions, phosphorylated slowly and
FT incompletely by DevS, decreased cooperative binding of
FT target DNA."
FT /evidence="ECO:0000269|PubMed:21764934"
FT MUTAGEN 104
FT /note="K->E: No phosphorylation by DevS (DosS)."
FT /evidence="ECO:0000269|PubMed:15073296"
FT MUTAGEN 198
FT /note="T->A: Decreases phosphorylation by PknH."
FT /evidence="ECO:0000269|PubMed:20630871"
FT MUTAGEN 205
FT /note="T->A: No phosphorylation by PknH."
FT /evidence="ECO:0000269|PubMed:20630871"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:3C3W"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:3C3W"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3C3W"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:3C3W"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3C3W"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 101..121
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 127..143
FT /evidence="ECO:0007829|PDB:3C3W"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:3C3W"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:3C57"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:3C57"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:3C57"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:3C3W"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3C3W"
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
