GRAS_STAA3
ID GRAS_STAA3 Reviewed; 346 AA.
AC Q2FIX9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Sensor protein kinase GraS;
DE EC=2.7.13.3;
DE AltName: Full=Glycopeptide resistance-associated protein S;
GN Name=graS; OrderedLocusNames=SAUSA300_0646;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
CC -!- FUNCTION: Member of the two-component regulatory system GraR/GraS
CC involved in resistance against cationic antimicrobial peptides (CAMPs).
CC Functions as a sensor protein kinase which phosphorylates GraR through
CC the auxiliary protein GraX. In turn, GraR up-regulates many genes such
CC as adhesins, exoproteins, transporters, toxins, and proteins involved
CC in cell wall synthesis. Down-regulates the expression of many genes
CC involved in RNA and amino acid synthesis or glycolysis.
CC {ECO:0000250|UniProtKB:Q2G0D9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Interacts with GraX. {ECO:0000250|UniProtKB:Q2G0D9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; CP000255; ABD22340.1; -; Genomic_DNA.
DR RefSeq; WP_001061252.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FIX9; -.
DR SMR; Q2FIX9; -.
DR PRIDE; Q2FIX9; -.
DR EnsemblBacteria; ABD22340; ABD22340; SAUSA300_0646.
DR KEGG; saa:SAUSA300_0646; -.
DR HOGENOM; CLU_000445_13_1_9; -.
DR OMA; YEWLRIH; -.
DR Proteomes; UP000001939; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..346
FT /note="Sensor protein kinase GraS"
FT /id="PRO_0000347926"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 126..332
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 346 AA; 41079 MW; 50820220FB5FDEAF CRC64;
MNNLKWVAYF LKSRMNWIFW ILFLNFLMLG ISLIDYDFPI DSLFYIVSLN LSLTMIFLLL
TYFKEVKLYK HFDKDKEIEE IKHKDLAETP FQRHTVDYLY RQISAHKEKV VEQQLQLNMH
EQTITEFVHD IKTPVTAMKL LIDQEKNQER KQALLYEWSR INSMLDTQLY ITRLESQRKD
MYFDYVSLKR MVIDEIQLTR HISQVKGIGF DVDFKVDDYV YTDIKWCRMI IRQILSNALK
YSENFNIEIG TELNDQHVSL YIKDYGRGIS KKDMPRIFER GFTSTANRNE TTSSGMGLYL
VNSVKDQLGI HLQVTSTVGK GTTVRLIFPL QNEIVERMSE VTNLSF