GRAS_STAA8
ID GRAS_STAA8 Reviewed; 346 AA.
AC Q2G0D9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Sensor histidine kinase GraS {ECO:0000303|PubMed:17676995};
DE EC=2.7.13.3;
DE AltName: Full=Glycopeptide resistance-associated protein S;
GN Name=graS {ECO:0000303|PubMed:17676995}; OrderedLocusNames=SAOUHSC_00666;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION IN CATIONIC ANTIMICROBIAL PEPTIDE RESISTANCE.
RX PubMed=17502406; DOI=10.1128/aac.00209-07;
RA Meehl M., Herbert S., Goetz F., Cheung A.;
RT "Interaction of the graRS two-component system with the vraFG ABC
RT transporter to support vancomycin-intermediate resistance in Staphylococcus
RT aureus.";
RL Antimicrob. Agents Chemother. 51:2679-2689(2007).
RN [3]
RP FUNCTION AS A GLOBAL REGULATOR.
RX PubMed=17676995; DOI=10.1371/journal.ppat.0030102;
RA Herbert S., Bera A., Nerz C., Kraus D., Peschel A., Goerke C., Meehl M.,
RA Cheung A., Goetz F.;
RT "Molecular basis of resistance to muramidase and cationic antimicrobial
RT peptide activity of lysozyme in staphylococci.";
RL PLoS Pathog. 3:981-994(2007).
RN [4]
RP FUNCTION IN CATIONIC ANTIMICROBIAL PEPTIDE RESISTANCE.
RX PubMed=18518949; DOI=10.1186/1471-2180-8-85;
RA Kraus D., Herbert S., Kristian S.A., Khosravi A., Nizet V., Goetz F.,
RA Peschel A.;
RT "The graRS regulatory system controls Staphylococcus aureus susceptibility
RT to antimicrobial host defenses.";
RL BMC Microbiol. 8:85-85(2008).
RN [5]
RP FUNCTION.
RX PubMed=21765893; DOI=10.1371/journal.pone.0021323;
RA Falord M., Maeder U., Hiron A., Debarbouille M., Msadek T.;
RT "Investigation of the Staphylococcus aureus GraSR regulon reveals novel
RT links to virulence, stress response and cell wall signal transduction
RT pathways.";
RL PLoS ONE 6:E21323-E21323(2011).
RN [6]
RP FUNCTION, AND INTERACTION WITH GRAX.
RX PubMed=25685323; DOI=10.12688/f1000research.5512.2;
RA Muzamal U., Gomez D., Kapadia F., Golemi-Kotra D.;
RT "Diversity of two-component systems: insights into the signal transduction
RT mechanism by the Staphylococcus aureus two-component system GraSR.";
RL F1000Research 3:252-252(2014).
CC -!- FUNCTION: Member of the two-component regulatory system GraR/GraS
CC involved in resistance against cationic antimicrobial peptides (CAMPs)
CC (PubMed:17502406, PubMed:18518949). Functions as a sensor protein
CC kinase which phosphorylates GraR through the auxiliary protein GraX
CC (PubMed:25685323). In turn, GraR up-regulates many genes such as
CC adhesins, exoproteins, transporters, toxins, and proteins involved in
CC cell wall synthesis (PubMed:21765893). Down-regulates the expression of
CC many genes involved in RNA and amino acid synthesis or glycolysis.
CC Confers resistance to vancomycin, polymyxin B, lysozyme and LL-37
CC (PubMed:17502406, PubMed:17676995, PubMed:18518949).
CC {ECO:0000269|PubMed:17502406, ECO:0000269|PubMed:17676995,
CC ECO:0000269|PubMed:18518949, ECO:0000269|PubMed:21765893,
CC ECO:0000269|PubMed:25685323}.
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:0000269|PubMed:25685323}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Does not seem to possess an autophosphorylation
CC activity. {ECO:0000269|PubMed:25685323}.
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DR EMBL; CP000253; ABD29799.1; -; Genomic_DNA.
DR RefSeq; WP_001061252.1; NZ_LS483365.1.
DR RefSeq; YP_499225.1; NC_007795.1.
DR AlphaFoldDB; Q2G0D9; -.
DR SMR; Q2G0D9; -.
DR STRING; 1280.SAXN108_0727; -.
DR EnsemblBacteria; ABD29799; ABD29799; SAOUHSC_00666.
DR GeneID; 3919429; -.
DR KEGG; sao:SAOUHSC_00666; -.
DR PATRIC; fig|93061.5.peg.597; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_13_1_9; -.
DR OMA; YEWLRIH; -.
DR PHI-base; PHI:7740; -.
DR PRO; PR:Q2G0D9; -.
DR Proteomes; UP000008816; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Virulence.
FT CHAIN 1..346
FT /note="Sensor histidine kinase GraS"
FT /id="PRO_0000347923"
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
