ID   GRAR_STAAB              Reviewed;         224 AA.
AC   Q2YSS2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Response regulator protein GraR;
DE   AltName: Full=Glycopeptide resistance-associated protein R;
GN   Name=graR; OrderedLocusNames=SAB0608;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80296.1; -; Genomic_DNA.
DR   RefSeq; WP_001166496.1; NC_007622.1.
DR   AlphaFoldDB; Q2YSS2; -.
DR   SMR; Q2YSS2; -.
DR   KEGG; sab:SAB0608; -.
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_0000347895"
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;  26094 MW;  54929D55B80B23DC CRC64;
     MQILLVEDDN TLFQELKKEL EQWDFNVAGI EDFGKVMDTF ESFNPEIVIL DVQLPKYDGF
     YWCRKMREVS NVPILFLSSR DNPMDQVMSM ELGADDYMQK PFYTNVLIAK LQAIYRRVYE
     FTAEEKRTLT WQDAIIDLSK DSIQKGDDTI FLSKTEMIIL EILITKKNQI VSRDTIITAL
     WDDEAFVSDN TLTVNVNRLR KKLSEISMDS AIETKVGKGY MAHE