VRAR_STAA1
ID VRAR_STAA1 Reviewed; 209 AA.
AC P0C0Z1; A7X405; Q9KWK7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Response regulator protein VraR;
GN Name=vraR; OrderedLocusNames=SAHV_1869;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10708580; DOI=10.1006/bbrc.2000.2277;
RA Kuroda M., Kuwahara-Arai K., Hiramatsu K.;
RT "Identification of the up- and down-regulated genes in vancomycin-resistant
RT Staphylococcus aureus strains Mu3 and Mu50 by cDNA differential
RT hybridization method.";
RL Biochem. Biophys. Res. Commun. 269:485-490(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31214151; DOI=10.3389/fmicb.2019.01222;
RA Dai Y., Gao C., Chen L., Chang W., Yu W., Ma X., Li J.;
RT "Heterogeneous Vancomycin-Intermediate Staphylococcus aureus uses the VraSR
RT regulatory system to modulate autophagy for increased intracellular
RT survival in macrophage-like cell line RAW264.7.";
RL Front. Microbiol. 10:1222-1222(2019).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31009806; DOI=10.1016/j.micinf.2019.04.003;
RA Gao C., Dai Y., Chang W., Fang C., Wang Z., Ma X.;
RT "VraSR has an important role in immune evasion of Staphylococcus aureus
RT with low level vancomycin resistance.";
RL Microbes Infect. 21:361-367(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
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 (PubMed:10708580). 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 (PubMed:31009806, PubMed:31214151).
CC {ECO:0000269|PubMed:10708580, ECO:0000269|PubMed:31009806,
CC ECO:0000269|PubMed:31214151}.
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}.
CC -!- DISRUPTION PHENOTYPE: Host cells show significantly lower
CC transcriptional levels of autophagy-related genes (PubMed:31214151). In
CC addition, VraS deletion decreases the ability of S.aureus to defend
CC against phagocytosis and killing by host polymorphonuclear leukocytes
CC (PMNs) (PubMed:31009806). {ECO:0000269|PubMed:31009806,
CC ECO:0000269|PubMed:31214151}.
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DR EMBL; AB035448; BAB03325.1; -; Genomic_DNA.
DR EMBL; AP009324; BAF78752.1; -; Genomic_DNA.
DR RefSeq; WP_000153535.1; NC_009782.1.
DR AlphaFoldDB; P0C0Z1; -.
DR SMR; P0C0Z1; -.
DR KEGG; saw:SAHV_1869; -.
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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; Antibiotic resistance; Cytoplasm; DNA-binding; Phosphoprotein;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..209
FT /note="Response regulator protein VraR"
FT /id="PRO_0000081268"
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
