ID   VRAR_STAAS              Reviewed;         209 AA.
AC   Q6G850;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Response regulator protein VraR;
GN   Name=vraR; OrderedLocusNames=SAS1806;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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
CC       expands and enhances the VraR binding to its own promoter leading to
CC       increased expression and subsequent modulation of as many as 40 genes,
CC       which ultimately constitute the S.aureus response to cell wall damage
CC       (By similarity). 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:P0C0Z1, ECO:0000250|UniProtKB:Q7A2Q1}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q7A2Q1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by VraS. Phosphorylation state of VraR controls
CC       dimerization of the protein. {ECO:0000250|UniProtKB:Q7A2Q1}.
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DR   EMBL; BX571857; CAG43611.1; -; Genomic_DNA.
DR   RefSeq; WP_000153535.1; NC_002953.3.
DR   AlphaFoldDB; Q6G850; -.
DR   SMR; Q6G850; -.
DR   KEGG; sas:SAS1806; -.
DR   HOGENOM; CLU_000445_90_10_9; -.
DR   OMA; NVLRKTQ; -.
DR   GO; GO:0005737; C:cytoplasm; 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; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..209
FT                   /note="Response regulator protein VraR"
FT                   /id="PRO_0000081273"
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"
SQ   SEQUENCE   209 AA;  23559 MW;  52984CE9494925B1 CRC64;
     MTIKVLFVDD HEMVRIGISS YLSTQSDIEV VGEGASGKEA IAKAHELKPD LILMDLLMED
     MDGVEATTQI KKDLPQIKVL MLTSFIEDKE VYRALDAGVD SYILKTTSAK DIADAVRKTS
     RGESVFEPEV LVKMRNRMKK RAELYEMLTE REMEILLLIA KGYSNQEIAS ASHITIKTVK
     THVSNILSKL EVQDRTQAVI YAFQHNLIQ