VRAR_STAAN
ID VRAR_STAAN Reviewed; 209 AA.
AC Q7A4R9; Q9KWK7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Response regulator protein VraR;
GN Name=vraR; OrderedLocusNames=SA1700;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kuroda-Murakami H., Kuroda M., Hiramatsu K.;
RT "Identification of differentially expressed genes of Staphylococcus aureus
RT in response to and in raised resistance to imipenem.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [3]
RP FUNCTION, AND REGULATION BY ANTIBIOTICS.
RX PubMed=12864861; DOI=10.1046/j.1365-2958.2003.03599.x;
RA Kuroda M., Kuroda H., Oshima T., Takeuchi F., Mori H., Hiramatsu K.;
RT "Two-component system VraSR positively modulates the regulation of cell-
RT wall biosynthesis pathway in Staphylococcus aureus.";
RL Mol. Microbiol. 49:807-821(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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:12864861). 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:0000269|PubMed:12864861}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q7A2Q1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by antibiotics (teicoplanin, ceftizoxime, imipenem,
CC bacitracin, D-cycloserine and vancomycin).
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; AB050859; BAB69827.1; -; Genomic_DNA.
DR EMBL; BA000018; BAB42970.1; -; Genomic_DNA.
DR PIR; C89976; C89976.
DR RefSeq; WP_000153535.1; NC_002745.2.
DR AlphaFoldDB; Q7A4R9; -.
DR SMR; Q7A4R9; -.
DR EnsemblBacteria; BAB42970; BAB42970; BAB42970.
DR KEGG; sau:SA1700; -.
DR HOGENOM; CLU_000445_90_10_9; -.
DR OMA; NVLRKTQ; -.
DR PHI-base; PHI:8948; -.
DR Proteomes; UP000000751; Chromosome.
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 1: Evidence at protein level;
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_0000081271"
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
