ID VRAS_STAAS Reviewed; 347 AA.
AC Q6G849;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Sensor protein VraS;
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:Q99SZ7};
GN Name=vraS; OrderedLocusNames=SAS1807;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
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DR EMBL; BX571857; CAG43612.1; -; Genomic_DNA.
DR RefSeq; WP_001017131.1; NC_002953.3.
DR AlphaFoldDB; Q6G849; -.
DR SMR; Q6G849; -.
DR KEGG; sas:SAS1807; -.
DR HOGENOM; CLU_000445_20_12_9; -.
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 CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF37; SIGNAL TRANSDUCTION HISTIDINE-PROTEIN KINASE_PHOSPHATASE UHPB; 1.
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; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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_0000074903"
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
//
