ID WALR_STAA8 Reviewed; 233 AA.
AC Q2G2U6; Q9XCM7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Transcriptional regulatory protein WalR {ECO:0000305};
GN Name=walR {ECO:0000303|PubMed:17827301}; Synonyms=yycF;
GN OrderedLocusNames=SAOUHSC_00020;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF GLU-63.
RX PubMed=10368139; DOI=10.1128/jb.181.12.3666-3673.1999;
RA Martin P.K., Li T., Sun D., Biek D.P., Schmid M.B.;
RT "Role in cell permeability of an essential two-component system in
RT Staphylococcus aureus.";
RL J. Bacteriol. 181:3666-3673(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION IN REGULATING ISAA, LYTM AND SSAA, DNA-BINDING, AND
RP PHOSPHORYLATION.
RX PubMed=14762013; DOI=10.1128/jb.186.4.1175-1181.2004;
RA Dubrac S., Msadek T.;
RT "Identification of genes controlled by the essential YycG/YycF two-
RT component system of Staphylococcus aureus.";
RL J. Bacteriol. 186:1175-1181(2004).
RN [4]
RP FUNCTION IN REGULATING CELL WALL METABOLISM, BIOFILM FORMATION, AND
RP AUTOLYSIS.
RX PubMed=17827301; DOI=10.1128/jb.00645-07;
RA Dubrac S., Boneca I.G., Poupel O., Msadek T.;
RT "New insights into the WalK/WalR (YycG/YycF) essential signal transduction
RT pathway reveal a major role in controlling cell wall metabolism and biofilm
RT formation in Staphylococcus aureus.";
RL J. Bacteriol. 189:8257-8269(2007).
RN [5]
RP FUNCTION.
RX PubMed=22825451; DOI=10.1128/iai.00195-12;
RA Delaune A., Dubrac S., Blanchet C., Poupel O., Maeder U., Hiron A.,
RA Leduc A., Fitting C., Nicolas P., Cavaillon J.M., Adib-Conquy M.,
RA Msadek T.;
RT "The WalKR system controls major staphylococcal virulence genes and is
RT involved in triggering the host inflammatory response.";
RL Infect. Immun. 80:3438-3453(2012).
CC -!- FUNCTION: Member of the two-component regulatory system WalK/WalR that
CC regulates genes involved in cell wall metabolism, virulence regulation,
CC biofilm production, oxidative stress resistance and antibiotic
CC resistance via direct or indirect regulation of autolysins
CC (PubMed:17827301, PubMed:22825451). Functions as a transcription
CC regulator by direct binding to promoter regions. Positively controls
CC the cell wall-hydrolytic activity through regulation of atlA and lytM,
CC as well as induces transcription of isaA, sceD, ssaA, and four ssaA-
CC related genes. Binds directly to the lytM, ssaA and isaA promoter
CC regions in vitro. {ECO:0000269|PubMed:10368139,
CC ECO:0000269|PubMed:14762013, ECO:0000269|PubMed:17827301,
CC ECO:0000269|PubMed:22825451}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by WalK (PubMed:14762013). Phosphorylated by PknB
CC on Thr-101 (By similarity). {ECO:0000250|UniProtKB:Q7A8E1,
CC ECO:0000269|PubMed:14762013}.
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DR EMBL; AF136709; AAD40237.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29209.1; -; Genomic_DNA.
DR RefSeq; WP_000101976.1; NZ_LS483365.1.
DR RefSeq; YP_498626.1; NC_007795.1.
DR AlphaFoldDB; Q2G2U6; -.
DR SMR; Q2G2U6; -.
DR STRING; 93061.SAOUHSC_00020; -.
DR PaxDb; 1280-SAXN108_0020; -.
DR GeneID; 3919191; -.
DR GeneID; 66838357; -.
DR KEGG; sao:SAOUHSC_00020; -.
DR PATRIC; fig|93061.5.peg.18; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_9; -.
DR OrthoDB; 9790442at2; -.
DR PHI-base; PHI:11718; -.
DR PRO; PR:Q2G2U6; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd17614; REC_OmpR_YycF-like; 1.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.690; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR047791; Resp_reg_WalR.
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 NCBIfam; NF040534; resp_reg_YycF; 1.
DR PANTHER; PTHR48111; REGULATOR OF RPOS; 1.
DR PANTHER; PTHR48111:SF76; TRANSCRIPTIONAL REGULATORY PROTEIN WALR; 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; C-terminal effector domain of the bipartite response regulators; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..233
FT /note="Transcriptional regulatory protein WalR"
FT /id="PRO_0000353042"
FT DOMAIN 4..117
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 132..231
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7A8E1"
FT MUTAGEN 63
FT /note="E->K: Fails to form colonies on rich and defined
FT media at temperatures above 40 degrees Celsius. Increased
FT susceptibility to linoleic acid and oleic acid. Increased
FT susceptibility to macrolide and lincosamide antibiotics."
FT /evidence="ECO:0000269|PubMed:10368139"
SQ SEQUENCE 233 AA; 27192 MW; BFA71D9C2464F600 CRC64;
MARKVVVVDD EKPIADILEF NLKKEGYDVY CAYDGNDAVD LIYEEEPDIV LLDIMLPGRD
GMEVCREVRK KYEMPIIMLT AKDSEIDKVL GLELGADDYV TKPFSTRELI ARVKANLRRH
YSQPAQDTGN VTNEITIKDI VIYPDAYSIK KRGEDIELTH REFELFHYLS KHMGQVMTRE
HLLQTVWGYD YFGDVRTVDV TIRRLREKIE DDPSHPEYIV TRRGVGYFLQ QHE
//
