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Database: UniProt
Entry: Q2FX09
LinkDB: Q2FX09
Original site: Q2FX09 
ID   VRAR_STAA8              Reviewed;         209 AA.
AC   Q2FX09;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-OCT-2019, entry version 95.
DE   RecName: Full=Response regulator protein VraR;
GN   Name=vraR; OrderedLocusNames=SAOUHSC_02098;
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press,
RL   Washington D.C. (2006).
RN   [2]
RP   FUNCTION, SUBUNIT, MUTAGENESIS OF MET-13, AND PHOSPHORYLATION.
RC   STRAIN=RN4220;
RX   PubMed=31277575; DOI=10.1186/s12866-019-1529-0;
RA   Tajbakhsh G., Golemi-Kotra D.;
RT   "The dimerization interface in VraR is essential for induction of the
RT   cell wall stress response in Staphylococcus aureus: a potential
RT   druggable target.";
RL   BMC Microbiol. 19:153-153(2019).
CC   -!- FUNCTION: Member of the two-component regulatory system VraS/VraR
CC       involved in the control of the cell wall peptidoglycan
CC       biosynthesis. Upon cellular stress, the histidine kinase VraS
CC       transfers the phosphoryl group onto VraR. Upon phosphorylation,
CC       VraR dimerizes at the N-terminal domain. In turn, phosphorylation-
CC       induced dimerization expand and enhance the VraR binding to its
CC       own promoter leading to increased expression and subsequent
CC       modulation of as many as 40 genes, which ultimately constitute the
CC       S.aureus response to cell wall damage (PubMed:31277575). In
CC       addition, inhibits the host autophagic flux and delays the early
CC       stage of autophagosome formation, thereby promoting bacterial
CC       survival. Facilitates the ability of S.aureus to resist host
CC       polymorphonuclear leukocytes-mediated phagocytosis and killing
CC       thus contributing to immune evasion (By similarity).
CC       {ECO:0000250|UniProtKB:Q9KWK8, ECO:0000269|PubMed:31277575}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31277575}.
CC   -!- PTM: Phosphorylated by VraS. Phosphorylation state of VraR
CC       controls dimerization of the protein.
CC       {ECO:0000269|PubMed:31277575}.
DR   EMBL; CP000253; ABD31148.1; -; Genomic_DNA.
DR   RefSeq; WP_000153530.1; NZ_LS483365.1.
DR   RefSeq; YP_500589.1; NC_007795.1.
DR   SMR; Q2FX09; -.
DR   STRING; 1280.SAXN108_1981; -.
DR   EnsemblBacteria; ABD31148; ABD31148; SAOUHSC_02098.
DR   GeneID; 3921170; -.
DR   KEGG; sao:SAOUHSC_02098; -.
DR   PATRIC; fig|93061.5.peg.1903; -.
DR   eggNOG; ENOG4105WH1; Bacteria.
DR   eggNOG; COG2197; LUCA.
DR   HOGENOM; HOG000034813; -.
DR   KO; K07694; -.
DR   OMA; NVLRKTQ; -.
DR   BioCyc; GCF_000013425:G1I0R-1986-MONOMER; -.
DR   BioCyc; SAUR93061:G1G5Y-1986-MONOMER; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   CDD; cd00156; REC; 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; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA-binding; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    209       Response regulator protein VraR.
FT                                /FTId=PRO_0000448243.
FT   DOMAIN        4    120       Response regulatory.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00169}.
FT   DOMAIN      141    206       HTH luxR-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   DNA_BIND    165    184       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   MOD_RES      55     55       4-aspartylphosphate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00169}.
FT   MUTAGEN      13     13       M->A: Loss of dimerization and binding to
FT                                target promoter.
FT                                {ECO:0000269|PubMed:31277575}.
SQ   SEQUENCE   209 AA;  23545 MW;  08385DE94859347A CRC64;
     MTIKVLFVDD HEMVRIGISS YLSTQSDIEV VGEGASGKEA IAKAHELKPD LILMDLLMDD
     MDGVEATTQI KKDLPQIKVL MLTSFIEDKE VYRALDAGVD SYILKTTSAK DIADAVRKTS
     RGESVFEPEV LVKMRNRMKK RAELYEMLTE REMEILLLIA KGYSNQEIAS ASHITIKTVK
     THVSNILSKL EVQDRTQAVI YAFQHNLIQ
//
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