ID   VRAS_STAA1              Reviewed;         347 AA.
AC   Q9KWK8; A7X407;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Sensor protein VraS;
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:Q99SZ7};
GN   Name=vraS; OrderedLocusNames=SAHV_1870;
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).
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:0000250|UniProtKB:Q99SZ7};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- PTM: Autophosphorylated on His-156. {ECO:0000250|UniProtKB:Q99SZ7}.
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DR   EMBL; AB035448; BAB03324.1; -; Genomic_DNA.
DR   EMBL; AP009324; BAF78753.1; -; Genomic_DNA.
DR   RefSeq; WP_001017146.1; NC_009782.1.
DR   AlphaFoldDB; Q9KWK8; -.
DR   SMR; Q9KWK8; -.
DR   KEGG; saw:SAHV_1870; -.
DR   HOGENOM; CLU_000445_20_12_9; -.
DR   OMA; FPDYCRQ; -.
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   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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..347
FT                   /note="Sensor protein VraS"
FT                   /id="PRO_0000074898"
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"
FT                   /evidence="ECO:0000250|UniProtKB:Q99SZ7"
SQ   SEQUENCE   347 AA;  40045 MW;  BBCE5837477A9083 CRC64;
     MNHYNRTIGS 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