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VRAR_STAAM
ID   VRAR_STAAM              Reviewed;         209 AA.
AC   Q7A2Q1;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Response regulator protein VraR;
GN   Name=vraR; OrderedLocusNames=SAV1884;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
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   [2]
RP   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   [3]
RP   FUNCTION, PHOSPHORYLATION AT ASP-55, SUBUNIT, AND MUTAGENESIS OF ASP-55.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=18326495; DOI=10.1074/jbc.m710010200;
RA   Belcheva A., Golemi-Kotra D.;
RT   "A close-up view of the VraSR two-component system. A mediator of
RT   Staphylococcus aureus response to cell wall damage.";
RL   J. Biol. Chem. 283:12354-12364(2008).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2-209, PHOSPHORYLATION, FUNCTION,
RP   AND SUBUNIT.
RX   PubMed=23650349; DOI=10.1073/pnas.1302819110;
RA   Leonard P.G., Golemi-Kotra D., Stock A.M.;
RT   "Phosphorylation-dependent conformational changes and domain rearrangements
RT   in Staphylococcus aureus VraR activation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:8525-8530(2013).
RN   [5]
RP   STRUCTURE BY NMR OF 138-209, AND SUBUNIT.
RX   PubMed=18293926; DOI=10.1021/bi701844q;
RA   Donaldson L.W.;
RT   "The NMR structure of the Staphylococcus aureus response regulator VraR DNA
RT   binding domain reveals a dynamic relationship between it and its associated
RT   receiver domain.";
RL   Biochemistry 47:3379-3388(2008).
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 (PubMed:18326495). Upon phosphorylation,
CC       VraR dimerizes at the N-terminal domain (PubMed:23650349,
CC       PubMed:18326495). In turn, phosphorylation-induced dimerization expands
CC       and enhances the VraR binding to its own promoter leading to increased
CC       expression and subsequent modulation of about 40 genes, which
CC       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 (By similarity).
CC       {ECO:0000250|UniProtKB:P0C0Z1, ECO:0000269|PubMed:10708580,
CC       ECO:0000269|PubMed:18326495, ECO:0000269|PubMed:23650349}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18293926,
CC       ECO:0000269|PubMed:18326495, ECO:0000269|PubMed:23650349}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by VraS. Phosphorylation state of VraR controls
CC       dimerization of the protein. {ECO:0000269|PubMed:18326495,
CC       ECO:0000269|PubMed:23650349}.
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DR   EMBL; BA000017; BAB58046.1; -; Genomic_DNA.
DR   RefSeq; WP_000153535.1; NC_002758.2.
DR   PDB; 2RNJ; NMR; -; A=138-209.
DR   PDB; 4GVP; X-ray; 2.03 A; A/B/C/D=2-209.
DR   PDB; 4IF4; X-ray; 2.35 A; A/B/C/D=2-209.
DR   PDBsum; 2RNJ; -.
DR   PDBsum; 4GVP; -.
DR   PDBsum; 4IF4; -.
DR   AlphaFoldDB; Q7A2Q1; -.
DR   SMR; Q7A2Q1; -.
DR   World-2DPAGE; 0002:Q7A2Q1; -.
DR   PaxDb; Q7A2Q1; -.
DR   EnsemblBacteria; BAB58046; BAB58046; SAV1884.
DR   KEGG; sav:SAV1884; -.
DR   HOGENOM; CLU_000445_90_10_9; -.
DR   OMA; NVLRKTQ; -.
DR   PhylomeDB; Q7A2Q1; -.
DR   BioCyc; SAUR158878:SAV_RS10310-MON; -.
DR   EvolutionaryTrace; Q7A2Q1; -.
DR   Proteomes; UP000002481; 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   3D-structure; Activator; Antibiotic resistance; Cytoplasm; DNA-binding;
KW   Phosphoprotein; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..209
FT                   /note="Response regulator protein VraR"
FT                   /id="PRO_0000081270"
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                   ECO:0000269|PubMed:18326495"
FT   MUTAGEN         55
FT                   /note="D->A: Complete loss of phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:18326495"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           12..24
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           37..47
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   STRAND          50..57
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   STRAND          77..84
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           88..96
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           109..120
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           131..143
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           144..147
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           150..160
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           165..172
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           176..189
FT                   /evidence="ECO:0007829|PDB:4GVP"
FT   HELIX           195..204
FT                   /evidence="ECO:0007829|PDB:4GVP"
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
 
 
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