GRAR_STAAC
ID GRAR_STAAC Reviewed; 224 AA.
AC Q5HI09;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
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=SACOL0716;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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 (By similarity) (PubMed:17502406). 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:17502406}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAW37780.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000046; AAW37780.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001166505.1; NC_002951.2.
DR AlphaFoldDB; Q5HI09; -.
DR SMR; Q5HI09; -.
DR EnsemblBacteria; AAW37780; AAW37780; SACOL0716.
DR KEGG; sac:SACOL0716; -.
DR HOGENOM; CLU_000445_30_3_9; -.
DR Proteomes; UP000000530; 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_0000347896"
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; 26079 MW; 50D2DCBAB6EBD323 CRC64;
MQILLVEDDN TLFQELKKEL EQWDFNVAGI EDFGKVMDTF ESFNPEIVIL DVQLPKYDGF
YWCRKMREVS NVPILFLSSR DNPMDQVMSM ELGADDYMQK PFYTNVLIAK LQAIYRRVYE
FTAEEKRTLT WQDAVVDLSK DSIQKGDQTI FLSKTEMIIL EILITKKNQI VSRDTIITAL
WDDEAFVSDN TLTVNVNRLR KKLSEISMDS AIETKVGKGY MAHE
