ID   WALR_STAAS              Reviewed;         233 AA.
AC   Q6GD72;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Transcriptional regulatory protein WalR {ECO:0000305};
GN   Name=walR; OrderedLocusNames=SAS0018;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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 (By
CC       similarity). Functions as a transcription regulator by direct binding
CC       to promoter regions (By similarity). {ECO:0000250|UniProtKB:Q2G2U6,
CC       ECO:0000250|UniProtKB:Q9RDT5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by WalK on Asp-53 (By similarity). Phosphorylated
CC       by PknB on Thr-101 (By similarity). {ECO:0000250|UniProtKB:Q7A8E1,
CC       ECO:0000250|UniProtKB:Q9RDT5}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG41790.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX571857; CAG41790.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000101976.1; NC_002953.3.
DR   AlphaFoldDB; Q6GD72; -.
DR   SMR; Q6GD72; -.
DR   GeneID; 66838357; -.
DR   KEGG; sas:SAS0018; -.
DR   HOGENOM; CLU_000445_30_4_9; -.
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   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; Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..233
FT                   /note="Transcriptional regulatory protein WalR"
FT                   /id="PRO_0000353037"
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"
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