ID   VRAS_STAAN              Reviewed;         347 AA.
AC   Q99SZ7;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Sensor protein VraS {ECO:0000303|PubMed:21173175};
DE            EC=2.7.13.3 {ECO:0000269|PubMed:21173175};
GN   Name=vraS {ECO:0000303|PubMed:21173175}; OrderedLocusNames=SA1701;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
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   [2]
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   [3]
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.
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT HIS-156, AND MUTAGENESIS
RP   OF HIS-156.
RX   PubMed=21173175; DOI=10.1128/aac.00720-10;
RA   Galbusera E., Renzoni A., Andrey D.O., Monod A., Barras C., Tortora P.,
RA   Polissi A., Kelley W.L.;
RT   "Site-specific mutation of Staphylococcus aureus VraS reveals a crucial
RT   role for the VraR-VraS sensor in the emergence of glycopeptide
RT   resistance.";
RL   Antimicrob. Agents Chemother. 55:1008-1020(2011).
RN   [5]
RP   FUNCTION, AND MUTAGENESIS OF GLU-276.
RX   PubMed=25899124; DOI=10.1038/ja.2015.42;
RA   Su J., Iehara M., Yasukawa J., Matsumoto Y., Hamamoto H., Sekimizu K.;
RT   "A novel mutation in the vraS gene of Staphylococcus aureus contributes to
RT   reduce susceptibility against daptomycin.";
RL   J. Antibiot. 68:646-648(2015).
CC   -!- FUNCTION: Member of the two-component regulatory system PprA/PprB
CC       involved in biofilm formation by controlling the expression of many
CC       related genes including type IVb pili major subunit flp pilin, adhesin
CC       bapA or cupE fimbriae. Modulates also quorum-sensing signal production
CC       acting on both negative and positive modulators. Functions as a heme
CC       sensor histidine kinase which is autophosphorylated at a histidine
CC       residue and transfers its phosphate group to PprB.
CC       {ECO:0000250|UniProtKB:Q9HWA7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:21173175};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Induced by antibiotics (teicoplanin, ceftizoxime, imipenem,
CC       bacitracin, D-cycloserine and vancomycin).
CC   -!- PTM: Autophosphorylated on His-156. {ECO:0000269|PubMed:21173175}.
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DR   EMBL; BA000018; BAB42971.1; -; Genomic_DNA.
DR   PIR; D89976; D89976.
DR   RefSeq; WP_001017131.1; NC_002745.2.
DR   AlphaFoldDB; Q99SZ7; -.
DR   SMR; Q99SZ7; -.
DR   EnsemblBacteria; BAB42971; BAB42971; BAB42971.
DR   KEGG; sau:SA1701; -.
DR   HOGENOM; CLU_000445_20_12_9; -.
DR   OMA; FPDYCRQ; -.
DR   PHI-base; PHI:8947; -.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR017202; LiaS/VraS.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   PIRSF; PIRSF037431; STHK_LiaS; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..347
FT                   /note="Sensor protein VraS"
FT                   /id="PRO_0000074901"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          150..341
FT                   /note="Histidine kinase"
FT   MOD_RES         156
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:21173175"
FT   MUTAGEN         156
FT                   /note="H->A: Complete loss of phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:21173175"
FT   MUTAGEN         276
FT                   /note="E->K: About 4-fold reduced daptomycin sensitivity."
FT                   /evidence="ECO:0000269|PubMed:25899124"
SQ   SEQUENCE   347 AA;  40045 MW;  E473F77F9330A3C0 CRC64;
     MNHYIRTIGS MLILVYSMLA AFLFIDKVFV NIIYFQGMFY TQIFGIPVFL FLNLIIILLC
     IIVGSVLAYK INQQNDWIKT QIERSMEGET VGINDQNIEI YSETLDLYHT LVPLNQELHK
     LRLKTQNLTN ENYNINDVKV KKIIEDERQR LARELHDSVS QQLFAASMML SAIKETKLEP
     PLDQQIPILE KMVQDSQLEM RALLLHLRPL GLKDKSLGEG IKDLVIDLQK KVPMKVVHEI
     QDFKVPKGIE DHLFRITQEA ISNTLRHSNG TKVTVELFNK DDYLLLRIQD NGKGFNVDEK
     LEQSYGLKNM RERALEIGAT FHIVSLPDSG TRIEVKAPLN KEDSYDD