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DMSR_HALVD
ID   DMSR_HALVD              Reviewed;         213 AA.
AC   D4GQ08; A0A384LDZ4; L9VI23;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Dimethyl sulfoxide reductase transcriptional activator {ECO:0000305};
DE            Short=DMSO reductase transcriptional activator {ECO:0000305};
DE   AltName: Full=DMSO-responsive regulator DmsR {ECO:0000303|PubMed:26507955};
DE   AltName: Full=DNA-binding protein DmsR {ECO:0000303|PubMed:26507955};
GN   Name=dmsR {ECO:0000303|PubMed:26507955, ECO:0000312|EMBL:ADE01457.1};
GN   OrderedLocusNames=HVO_B0361 {ECO:0000312|EMBL:ADE01457.1};
GN   ORFNames=C498_01850 {ECO:0000312|EMBL:ELY36850.1};
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG   Plasmid pHV3 {ECO:0000312|EMBL:ADE01457.1,
OG   ECO:0000312|Proteomes:UP000008243}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800 {ECO:0000312|EMBL:ADE01457.1};
RN   [1] {ECO:0000312|EMBL:ADE01457.1, ECO:0000312|Proteomes:UP000008243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2 {ECO:0000312|Proteomes:UP000008243};
RC   PLASMID=pHV3 {ECO:0000312|EMBL:ADE01457.1};
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2] {ECO:0000312|EMBL:ELY36850.1, ECO:0000312|Proteomes:UP000011532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2 {ECO:0000312|Proteomes:UP000011532};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DS2 / DS70 {ECO:0000303|PubMed:26507955};
RX   PubMed=26507955; DOI=10.1007/s00792-015-0794-6;
RA   Qi Q., Ito Y., Yoshimatsu K., Fujiwara T.;
RT   "Transcriptional regulation of dimethyl sulfoxide respiration in a
RT   haloarchaeon, Haloferax volcanii.";
RL   Extremophiles 20:27-36(2016).
CC   -!- FUNCTION: Involved in activating dmsEABCD gene expression related to
CC       dimethyl sulfoxide (DMSO) reductase. Required for anaerobic respiration
CC       on dimethyl sulfoxide (DMSO). {ECO:0000269|PubMed:26507955}.
CC   -!- INDUCTION: By anaerobical conditions and dimethyl sulfoxide (DMSO).
CC       {ECO:0000269|PubMed:26507955}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no dimethyl
CC       sulfoxide (DMSO) reductase activity under aerobic, anaerobic without
CC       substrate, anaerobic with DMSO as substrate nor under anaerobic with
CC       nitrate as substrate conditions. Cells are not able to grow
CC       anaerobically by dimethyl sulfoxide (DMSO) respiration. DMSO does not
CC       activate transcription of the dmsEABCD genes induced by the anaerobic
CC       conditions. No effect on aerobical growth or growth under denitrifying
CC       conditions. {ECO:0000269|PubMed:26507955}.
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DR   EMBL; CP001953; ADE01457.1; -; Genomic_DNA.
DR   EMBL; AOHU01000021; ELY36850.1; -; Genomic_DNA.
DR   RefSeq; WP_004041174.1; NZ_AOHU01000021.1.
DR   STRING; 309800.C498_01850; -.
DR   EnsemblBacteria; ADE01457; ADE01457; HVO_B0361.
DR   EnsemblBacteria; ELY36850; ELY36850; C498_01850.
DR   GeneID; 8919166; -.
DR   KEGG; hvo:HVO_B0361; -.
DR   PATRIC; fig|309800.29.peg.357; -.
DR   eggNOG; arCOG02281; Archaea.
DR   HOGENOM; CLU_109670_1_0_2; -.
DR   OMA; AFSEVGC; -.
DR   OrthoDB; 70649at2157; -.
DR   Proteomes; UP000008243; Plasmid pHV3.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IC:UniProtKB.
DR   GO; GO:1904620; P:cellular response to dimethyl sulfoxide; IEP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0036293; P:response to decreased oxygen levels; IEP:UniProtKB.
DR   InterPro; IPR007050; HTH_bacterioopsin.
DR   Pfam; PF04967; HTH_10; 1.
PE   2: Evidence at transcript level;
KW   Activator; Plasmid; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..213
FT                   /note="Dimethyl sulfoxide reductase transcriptional
FT                   activator"
FT                   /id="PRO_0000454759"
FT   DOMAIN          155..206
FT                   /note="HTH bat-type"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   213 AA;  22958 MW;  3D07C123BFC652F2 CRC64;
     MADSTSGVAE AKADTLREQH LQLLLEIEPA KRCSCPLAGP DSAVEDVHTQ LDGDVCHAEV
     TVGDGDASKV VHATTSVGDD CLCRAFAEFE CVPRIRRADG ECIVVETYLS DRAVITDLVE
     RLDELTERVC LRRLTSDGRG DSTESKTATI DLSSLTAKQR EAALIAVHHG YYETPRRTEL
     ATLAEALGIS KSALSQRLNA VEAKLATAVF DSE
 
 
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