ID   VRAS_STAES              Reviewed;         348 AA.
AC   Q8CRV2;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Sensor protein VraS;
DE            EC=2.7.13.3;
GN   Name=vraS; OrderedLocusNames=SE_1570;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Member of the two-component regulatory system VraS/VraR
CC       involved in the control of the cell wall peptidoglycan biosynthesis.
CC       Probably activates VraR by phosphorylation (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AE015929; AAO05169.1; -; Genomic_DNA.
DR   RefSeq; NP_765125.1; NC_004461.1.
DR   RefSeq; WP_001830374.1; NZ_WBME01000010.1.
DR   AlphaFoldDB; Q8CRV2; -.
DR   SMR; Q8CRV2; -.
DR   STRING; 176280.SE_1570; -.
DR   EnsemblBacteria; AAO05169; AAO05169; SE_1570.
DR   GeneID; 50018330; -.
DR   KEGG; sep:SE_1570; -.
DR   PATRIC; fig|176280.10.peg.1534; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_12_9; -.
DR   OMA; FPDYCRQ; -.
DR   Proteomes; UP000001411; 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   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..348
FT                   /note="Sensor protein VraS"
FT                   /id="PRO_0000074906"
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"
SQ   SEQUENCE   348 AA;  40066 MW;  8BD5768F8DF260D7 CRC64;
     MNHYIRAIGS MLILVYSMLI AFLFIDKVFV NIIFFQGMFY TQIFGIPVFL FLNLLIVLLC
     IIVGSVLAYK INQQNDWIIS QIERSIEGQT VGINDQNIEL YTETIDIYHT LVPLNQELHR
     LRMKTQNLTN ENYNINDVKV KKIIEDERQR LARELHDSVS QQLFAASMML SAIKESKLEP
     PLNQQIPILE KMVQDSQLEM RALLLHLRPI GLKDKSLGEG IKDLVIDLQK KVPMKVVHEI
     QDFEVPKGIE DHLFRITQEA ISNTLRHSNG TKVTVELFNQ EDYLLLRIQD NGKGFNVDEK
     FEQSYGLKNM RERALEIGAT FHIVSLPDSG TRIEVKAPLN KEENSSGD