VRAS_STAAM
ID VRAS_STAAM Reviewed; 347 AA.
AC Q7A2Q0;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sensor protein VraS;
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:Q99SZ7};
GN Name=vraS; OrderedLocusNames=SAV1885;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION.
RX PubMed=10708580; DOI=10.1006/bbrc.2000.2277;
RA Kuroda M., Kuwahara-Arai K., Hiramatsu K.;
RT "Identification of the up- and down-regulated genes in vancomycin-resistant
RT Staphylococcus aureus strains Mu3 and Mu50 by cDNA differential
RT hybridization method.";
RL Biochem. Biophys. Res. Commun. 269:485-490(2000).
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; BA000017; BAB58047.1; -; Genomic_DNA.
DR RefSeq; WP_001017146.1; NC_002758.2.
DR PDB; 4GT8; X-ray; 1.51 A; A=212-347.
DR PDBsum; 4GT8; -.
DR AlphaFoldDB; Q7A2Q0; -.
DR SMR; Q7A2Q0; -.
DR PaxDb; Q7A2Q0; -.
DR EnsemblBacteria; BAB58047; BAB58047; SAV1885.
DR KEGG; sav:SAV1885; -.
DR HOGENOM; CLU_000445_20_12_9; -.
DR OMA; FPDYCRQ; -.
DR PhylomeDB; Q7A2Q0; -.
DR BioCyc; SAUR158878:SAV_RS10315-MON; -.
DR Proteomes; UP000002481; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..347
FT /note="Sensor protein VraS"
FT /id="PRO_0000074900"
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"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:4GT8"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:4GT8"
FT HELIX 247..267
FT /evidence="ECO:0007829|PDB:4GT8"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:4GT8"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:4GT8"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:4GT8"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4GT8"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:4GT8"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:4GT8"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:4GT8"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:4GT8"
SQ SEQUENCE 347 AA; 40045 MW; BBCE5837477A9083 CRC64;
MNHYNRTIGS 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
