ID   VRAS_STAS1              Reviewed;         347 AA.
AC   Q49YT0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Sensor protein VraS;
DE            EC=2.7.13.3;
GN   Name=vraS; OrderedLocusNames=SSP0908;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18053.1; -; Genomic_DNA.
DR   RefSeq; WP_011302781.1; NZ_MTGA01000031.1.
DR   AlphaFoldDB; Q49YT0; -.
DR   SMR; Q49YT0; -.
DR   STRING; 342451.SSP0908; -.
DR   EnsemblBacteria; BAE18053; BAE18053; SSP0908.
DR   GeneID; 66867063; -.
DR   KEGG; ssp:SSP0908; -.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_12_9; -.
DR   OMA; FPDYCRQ; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000006371; 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..347
FT                   /note="Sensor protein VraS"
FT                   /id="PRO_0000074908"
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   347 AA;  40051 MW;  747AAB6D6E038D3C CRC64;
     MNHYFRAIGS MLILVYSTFF AIFFIDKVFV NIMYFQGMFY TQIFGIPVLL FLNLMVILLC
     IIVGSVLAYK INQQNHWLKD QIERSIEGQT VGINDQNIEL YNETIELYQT LVPLNQEVHK
     LRMKTQNLTN ESYNINDVKV KKIIEDERQR LARELHDSVS QQLFAASMML SAIKETELKA
     PLDQQIPVLE KMIQDSQLEM RALLLHLRPI GLKDKSLGEG IKDLVVDLQK KVPMKVVHDI
     EEFKVPKGIE DHLFRITQEA ISNTLRHSKG TKVTIELFNR EEYLLLRIQD NGKGFNVDDK
     VEQSYGLKNM RERALEIGAT FHIVSLPDAG TRIEVKAPLN KEDSNAD