ID   VRAS_STAEQ              Reviewed;         348 AA.
AC   Q5HN49;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Sensor protein VraS;
DE            EC=2.7.13.3;
GN   Name=vraS; OrderedLocusNames=SERP1423;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW54787.1; -; Genomic_DNA.
DR   RefSeq; WP_001830374.1; NC_002976.3.
DR   AlphaFoldDB; Q5HN49; -.
DR   SMR; Q5HN49; -.
DR   STRING; 176279.SERP1423; -.
DR   EnsemblBacteria; AAW54787; AAW54787; SERP1423.
DR   GeneID; 50018330; -.
DR   KEGG; ser:SERP1423; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_12_9; -.
DR   OMA; FPDYCRQ; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..348
FT                   /note="Sensor protein VraS"
FT                   /id="PRO_0000074905"
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