ID   GRAR_STAAM              Reviewed;         224 AA.
AC   Q932F1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Response regulator protein GraR;
DE   AltName: Full=Glycopeptide resistance-associated protein R;
GN   Name=graR; OrderedLocusNames=SAV0659;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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).
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; BA000017; BAB56821.1; -; Genomic_DNA.
DR   RefSeq; WP_001166501.1; NC_002758.2.
DR   AlphaFoldDB; Q932F1; -.
DR   SMR; Q932F1; -.
DR   PaxDb; Q932F1; -.
DR   EnsemblBacteria; BAB56821; BAB56821; SAV0659.
DR   KEGG; sav:SAV0659; -.
DR   HOGENOM; CLU_000445_30_3_9; -.
DR   OMA; QIISEVW; -.
DR   PhylomeDB; Q932F1; -.
DR   BioCyc; SAUR158878:SAV_RS03630-MON; -.
DR   Proteomes; UP000002481; Chromosome.
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   1: Evidence at protein level;
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_0000347902"
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;  26039 MW;  4A636CA67737D233 CRC64;
     MQILLVEDDN TLFQELKKEL EQWDFNVAGI EDFGKVMDTF ESFNPEIVIL DVQLPKYDGF
     YWCRKMREVS NVPILFLSSR DNPMDQVMSM ELGADDYMQK PFYTNVLIAK LQAIYRRVYE
     FTAEEKRTLT WQDAVVDLSK DSIQKGDDTI FLSKTEMIIL EILITKKNQI VSRDTIITAL
     WDDEAFVSDN TLTVNVSRLR KKLSEISMDS AIETKVGKGY MAHE