ID   VRAS_STAHJ              Reviewed;         348 AA.
AC   Q4L7J6;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Sensor protein VraS;
DE            EC=2.7.13.3;
GN   Name=vraS; OrderedLocusNames=SH1070;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04379.1; -; Genomic_DNA.
DR   RefSeq; WP_011275375.1; NC_007168.1.
DR   AlphaFoldDB; Q4L7J6; -.
DR   SMR; Q4L7J6; -.
DR   STRING; 279808.SH1070; -.
DR   EnsemblBacteria; BAE04379; BAE04379; SH1070.
DR   GeneID; 58062756; -.
DR   KEGG; sha:SH1070; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_12_9; -.
DR   OMA; FPDYCRQ; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000000543; 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_0000074907"
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;  40180 MW;  6801EEC340E4C078 CRC64;
     MNHYLRAIGS MLILVYSMLT AFLFIDKVFV NIIYFQGMFY TQIFGIPVFL FLNLVIILLC
     IIVGSILAYK INQQNQWIKS QIEHAIEGET VGINDQNIEL YNETIDLYQT LVPLNQELHR
     LRMKTQNLTN ENYNMNDVKV KKIIENERQR LARELHDSVS QQLFAASMML SAIKETKLEA
     PLDQQIPVLE KMVQESQLEM RALLLHLRPL GLKDKSLGEG IKDLVIDLQK KVPMKVIHDI
     QDFKVPKGIE DHLFRITQEA ISNTLRHSNG TKVTVELFNQ QDYLLLRIQD NGKGFNVDEK
     LEQSYGLKNM RERALEIGAT FHIVSLPDSG TRIEVKAPLN REDDNNDD