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   25-MAY-2022, entry version 104.
DE   RecName: Full=Response regulator protein VraR;
GN   Name=vraR; OrderedLocusNames=SAOUHSC_02098;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
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 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., 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, Washington
RL   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 cell
RT   wall stress response in Staphylococcus aureus: a potential druggable
RT   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 biosynthesis.
CC       Upon cellular stress, the histidine kinase VraS transfers the
CC       phosphoryl group onto VraR. Upon phosphorylation, VraR dimerizes at the
CC       N-terminal domain. In turn, phosphorylation-induced dimerization expand
CC       and enhance the VraR binding to its own promoter leading to increased
CC       expression and subsequent modulation of as many as 40 genes, which
CC       ultimately constitute the S.aureus response to cell wall damage
CC       (PubMed:31277575). In addition, inhibits the host autophagic flux and
CC       delays the early stage of autophagosome formation, thereby promoting
CC       bacterial survival. Facilitates the ability of S.aureus to resist host
CC       polymorphonuclear leukocytes-mediated phagocytosis and killing thus
CC       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 controls
CC       dimerization of the protein. {ECO:0000269|PubMed:31277575}.
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DR   EMBL; CP000253; ABD31148.1; -; Genomic_DNA.
DR   RefSeq; WP_000153530.1; NZ_LS483365.1.
DR   RefSeq; YP_500589.1; NC_007795.1.
DR   AlphaFoldDB; Q2FX09; -.
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; COG2197; Bacteria.
DR   HOGENOM; CLU_000445_90_10_9; -.
DR   OMA; NVLRKTQ; -.
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   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   DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..209
FT                   /note="Response regulator protein VraR"
FT                   /id="PRO_0000448243"
FT   DOMAIN          4..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          141..206
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   DNA_BIND        165..184
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   MOD_RES         55
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MUTAGEN         13
FT                   /note="M->A: Loss of dimerization and binding to target
FT                   promoter."
FT                   /evidence="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