ID   VRAS_STAAC              Reviewed;         347 AA.
AC   Q5HEN9;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Sensor protein VraS;
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:Q99SZ7};
GN   Name=vraS; OrderedLocusNames=SACOL1943;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
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 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000046; AAW38384.1; -; Genomic_DNA.
DR   RefSeq; WP_001017131.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEN9; -.
DR   SMR; Q5HEN9; -.
DR   EnsemblBacteria; AAW38384; AAW38384; SACOL1943.
DR   KEGG; sac:SACOL1943; -.
DR   HOGENOM; CLU_000445_20_12_9; -.
DR   OMA; FPDYCRQ; -.
DR   Proteomes; UP000000530; 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..347
FT                   /note="Sensor protein VraS"
FT                   /id="PRO_0000074899"
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;  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