ID   GRAR_STAAS              Reviewed;         224 AA.
AC   Q6GBH1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Response regulator protein GraR;
DE   AltName: Full=Glycopeptide resistance-associated protein R;
GN   Name=graR; OrderedLocusNames=SAS0624;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; 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 GraR/GraS
CC       involved in resistance against cationic antimicrobial peptides (CAMPs).
CC       Upon phosphorylation by GraS, functions as a transcription regulator by
CC       direct binding to promoter regions of target genes such as adhesins,
CC       exoproteins, transporters, toxins, and proteins involved in cell wall
CC       synthesis. Down-regulates the expression of many genes involved in RNA
CC       and amino acid synthesis or glycolysis. {ECO:0000250|UniProtKB:Q2G0E0}.
CC   -!- SUBUNIT: Interacts with GraX. {ECO:0000250|UniProtKB:Q2G0D9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated by GraS. Phosphorylated by Stk1; phosphorylation
CC       increases the DNA-binding activity of GraR.
CC       {ECO:0000250|UniProtKB:Q2G0E0}.
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DR   EMBL; BX571857; CAG42400.1; -; Genomic_DNA.
DR   RefSeq; WP_001166500.1; NC_002953.3.
DR   AlphaFoldDB; Q6GBH1; -.
DR   SMR; Q6GBH1; -.
DR   KEGG; sas:SAS0624; -.
DR   HOGENOM; CLU_000445_30_3_9; -.
DR   OMA; QIISEVW; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; PTHR48111; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Activator; Antibiotic resistance; Cytoplasm; DNA-binding; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation;
KW   Two-component regulatory system; Virulence.
FT   CHAIN           1..224
FT                   /note="Response regulator protein GraR"
FT                   /id="PRO_0000347900"
FT   DOMAIN          2..115
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        126..224
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT   MOD_RES         51
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         128
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2G0E0"
FT   MOD_RES         130
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2G0E0"
FT   MOD_RES         149
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2G0E0"
SQ   SEQUENCE   224 AA;  26066 MW;  4A636CBAA6FAD233 CRC64;
     MQILLVEDDN TLFQELKKEL EQWDFNVAGI EDFGKVMDTF ESFNPEIVIL DVQLPKYDGF
     YWCRKMREVS NVPILFLSSR DNPMDQVMSM ELGADDYMQK PFYTNVLIAK LQAIYRRVYE
     FTAEEKRTLT WQDAVVDLSK DSIQKGDDTI FLSKTEMIIL EILITKKNQI VSRDTIITAL
     WDDEAFVSDN TLTVNVNRLR KKLSEISMDS AIETKVGKGY MAHE