GRAR_STAAW
ID GRAR_STAAW Reviewed; 224 AA.
AC Q7A1L2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Response regulator protein GraR;
DE AltName: Full=Glycopeptide resistance-associated protein R;
GN Name=graR; OrderedLocusNames=MW0621;
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, AND DISRUPTION PHENOTYPE.
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). Upon phosphorylation by GraS,
CC functions as a transcription regulator by direct binding to promoter
CC regions of target genes such as adhesins, exoproteins, transporters,
CC toxins, and proteins involved in cell wall synthesis. Down-regulates
CC the expression of many genes involved in RNA and amino acid synthesis
CC or glycolysis (By similarity). {ECO:0000250|UniProtKB:Q2G0E0,
CC ECO:0000269|PubMed:25287929, ECO:0000269|PubMed:26597988}.
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}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000033; BAB94486.1; -; Genomic_DNA.
DR RefSeq; WP_001166500.1; NC_003923.1.
DR AlphaFoldDB; Q7A1L2; -.
DR SMR; Q7A1L2; -.
DR EnsemblBacteria; BAB94486; BAB94486; BAB94486.
DR KEGG; sam:MW0621; -.
DR HOGENOM; CLU_000445_30_3_9; -.
DR OMA; QIISEVW; -.
DR Proteomes; UP000000418; 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 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_0000347903"
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
