GRAS_STAAW
ID GRAS_STAAW Reviewed; 346 AA.
AC Q8NXR5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=MW0622;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-37 AND PRO-39.
RX PubMed=25287929; DOI=10.1128/iai.02480-14;
RA Cheung A.L., Bayer A.S., Yeaman M.R., Xiong Y.Q., Waring A.J., Memmi G.,
RA Donegan N., Chaili S., Yang S.J.;
RT "Site-specific mutation of the sensor kinase GraS in Staphylococcus aureus
RT alters the adaptive response to distinct cationic antimicrobial peptides.";
RL Infect. Immun. 82:5336-5345(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26597988; DOI=10.1128/iai.01030-15;
RA Chaili S., Cheung A.L., Bayer A.S., Xiong Y.Q., Waring A.J., Memmi G.,
RA Donegan N., Yang S.J., Yeaman M.R.;
RT "The GraS Sensor in Staphylococcus aureus Mediates Resistance to Host
RT Defense Peptides Differing in Mechanisms of Action.";
RL Infect. Immun. 84:459-466(2016).
CC -!- FUNCTION: Member of the two-component regulatory system GraR/GraS
CC involved in resistance against cationic antimicrobial peptides (CAMPs)
CC (PubMed:25287929, PubMed:26597988). Functions as a sensor protein
CC kinase which phosphorylates GraR through the auxiliary protein GraX. In
CC turn, GraR up-regulates many genes such as adhesins, exoproteins,
CC transporters, toxins, and proteins involved in cell wall synthesis.
CC Down-regulates the expression of many genes involved in RNA and amino
CC acid synthesis or glycolysis (By similarity).
CC {ECO:0000250|UniProtKB:Q2G0D9, ECO:0000269|PubMed:25287929,
CC ECO:0000269|PubMed:26597988}.
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}.
CC -!- DISRUPTION PHENOTYPE: Deletion leads to complete loss of resistance
CC towards host cationic antimicrobial peptides (CAPs).
CC {ECO:0000269|PubMed:25287929, ECO:0000269|PubMed:26597988}.
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DR EMBL; BA000033; BAB94487.1; -; Genomic_DNA.
DR RefSeq; WP_001061262.1; NC_003923.1.
DR AlphaFoldDB; Q8NXR5; -.
DR SMR; Q8NXR5; -.
DR EnsemblBacteria; BAB94487; BAB94487; BAB94487.
DR KEGG; sam:MW0622; -.
DR HOGENOM; CLU_000445_13_1_9; -.
DR OMA; YEWLRIH; -.
DR Proteomes; UP000000418; 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 1: Evidence at protein level;
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_0000347921"
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"
FT MUTAGEN 37
FT /note="D->A: About 50% increased resistance to host
FT cationic antimicrobial peptides."
FT /evidence="ECO:0000269|PubMed:25287929"
FT MUTAGEN 39
FT /note="P->A: About 50% decreased resistance to host
FT cationic antimicrobial peptides."
FT /evidence="ECO:0000269|PubMed:25287929"
FT MUTAGEN 39
FT /note="P->S: About 50% decreased resistance to host
FT cationic antimicrobial peptides."
FT /evidence="ECO:0000269|PubMed:25287929"
SQ SEQUENCE 346 AA; 41045 MW; 536522F060D7CDA8 CRC64;
MNNLKWVAYF LKSRMNWIFW ILFLNLLMLG ISLIDYDFPI DSLFYIVSLN LSLTMIFLIL
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
