WALR_STAAU
ID WALR_STAAU Reviewed; 233 AA.
AC Q9RDT5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Transcriptional regulatory protein WalR {ECO:0000305};
GN Name=walR; Synonyms=vicR, yycF;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12379689; DOI=10.1128/iai.70.11.6121-6128.2002;
RA Wagner C., de Saizieu A., Schoenfeld H.-J., Kamber M., Lange R.,
RA Thompson C.J., Page M.G.;
RT "Genetic analysis and functional characterization of the Streptococcus
RT pneumoniae vic operon.";
RL Infect. Immun. 70:6121-6128(2002).
RN [2]
RP PHOSPHORYLATION.
RC STRAIN=WCUH29 / NCIMB 40771;
RX PubMed=12867749; DOI=10.1159/000071077;
RA Clausen V.A., Bae W., Throup J., Burnham M.K.R., Rosenberg M., Wallis N.G.;
RT "Biochemical characterization of the first essential two-component signal
RT transduction system from Staphylococcus aureus and Streptococcus
RT pneumoniae.";
RL J. Mol. Microbiol. Biotechnol. 5:252-260(2003).
RN [3]
RP OVEREXPRESSION.
RC STRAIN=SA137/93A;
RX PubMed=17418637; DOI=10.1016/j.ijmm.2007.02.002;
RA Jansen A., Tuerck M., Szekat C., Nagel M., Clever I., Bierbaum G.;
RT "Role of insertion elements and yycFG in the development of decreased
RT susceptibility to vancomycin in Staphylococcus aureus.";
RL Int. J. Med. Microbiol. 297:205-215(2007).
RN [4]
RP FUNCTION, PHOSPHORYLATION AT ASP-53, AND MUTAGENESIS OF ASP-53.
RX PubMed=31296851; DOI=10.1038/s41467-019-10932-4;
RA Monk I.R., Shaikh N., Begg S.L., Gajdiss M., Sharkey L.K.R., Lee J.Y.H.,
RA Pidot S.J., Seemann T., Kuiper M., Winnen B., Hvorup R., Collins B.M.,
RA Bierbaum G., Udagedara S.R., Morey J.R., Pulyani N., Howden B.P.,
RA Maher M.J., McDevitt C.A., King G.F., Stinear T.P.;
RT "Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK
RT histidine kinase of Staphylococcus aureus.";
RL Nat. Commun. 10:3067-3067(2019).
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:31296851). Functions as a transcription regulator by direct
CC binding to promoter regions (By similarity).
CC {ECO:0000250|UniProtKB:Q2G2U6, ECO:0000269|PubMed:31296851}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by WalK on Asp-53 (PubMed:12867749,
CC PubMed:31296851). Phosphorylated by PknB on Thr-101 (By similarity).
CC {ECO:0000250|UniProtKB:Q7A8E1, ECO:0000269|PubMed:12867749,
CC ECO:0000269|PubMed:31296851}.
CC -!- MISCELLANEOUS: Overexpression of walK/walR reduces susceptibility
CC against vancomycin. {ECO:0000269|PubMed:17418637}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB65399.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ012052; CAB65399.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000101976.1; NZ_WYDB01000001.1.
DR PDB; 2ZXJ; X-ray; 1.87 A; A/B=123-233.
DR PDBsum; 2ZXJ; -.
DR AlphaFoldDB; Q9RDT5; -.
DR SMR; Q9RDT5; -.
DR GeneID; 66838357; -.
DR OMA; IDRVWGS; -.
DR EvolutionaryTrace; Q9RDT5; -.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Phosphoprotein;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..233
FT /note="Transcriptional regulatory protein WalR"
FT /id="PRO_0000353031"
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 ECO:0000269|PubMed:31296851"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7A8E1"
FT MUTAGEN 53
FT /note="D->A: Loss of phosphorylation by WalK."
FT /evidence="ECO:0000269|PubMed:31296851"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:2ZXJ"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2ZXJ"
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
