LYTR_STAA8
ID LYTR_STAA8 Reviewed; 246 AA.
AC P60611; P96456; Q2G1B4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Transcriptional regulatory protein LytR;
GN Name=lytR; OrderedLocusNames=SAOUHSC_00231;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8550490; DOI=10.1128/jb.178.3.611-618.1996;
RA Brunskill E.W., Bayles K.W.;
RT "Identification and molecular characterization of a putative regulatory
RT locus that affects autolysis in Staphylococcus aureus.";
RL J. Bacteriol. 178:611-618(1996).
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 REGULATION OF LRGA AND LRGB.
RX PubMed=8824633; DOI=10.1128/jb.178.19.5810-5812.1996;
RA Brunskill E.W., Bayles K.W.;
RT "Identification of LytSR-regulated genes from Staphylococcus aureus.";
RL J. Bacteriol. 178:5810-5812(1996).
RN [4]
RP FUNCTION.
RC STRAIN=UAMS-1;
RX PubMed=19502411; DOI=10.1128/jb.00348-09;
RA Sharma-Kuinkel B.K., Mann E.E., Ahn J.S., Kuechenmeister L.J., Dunman P.M.,
RA Bayles K.W.;
RT "The Staphylococcus aureus LytSR two-component regulatory system affects
RT biofilm formation.";
RL J. Bacteriol. 191:4767-4775(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=UAMS-1;
RX PubMed=23733465; DOI=10.1128/aac.00412-13;
RA Yang S.J., Xiong Y.Q., Yeaman M.R., Bayles K.W., Abdelhady W., Bayer A.S.;
RT "Role of the LytSR two-component regulatory system in adaptation to
RT cationic antimicrobial peptides in Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 57:3875-3882(2013).
RN [6]
RP FUNCTION, MUTAGENESIS OF ASP-53, AND PHOSPHORYLATION.
RC STRAIN=UAMS-1;
RX PubMed=25491472; DOI=10.1111/mmi.12902;
RA Lehman M.K., Bose J.L., Sharma-Kuinkel B.K., Moormeier D.E., Endres J.L.,
RA Sadykov M.R., Biswas I., Bayles K.W.;
RT "Identification of the amino acids essential for LytSR-mediated signal
RT transduction in Staphylococcus aureus and their roles in biofilm-specific
RT gene expression.";
RL Mol. Microbiol. 95:723-737(2015).
CC -!- FUNCTION: Member of the two-component regulatory system LytR/LytS that
CC regulates genes involved in autolysis, programmed cell death, biofilm
CC formation and cell wall metabolism (PubMed:19502411). Participates also
CC in sensing and responding to host defense cationic antimicrobial
CC peptides (HDPs) (PubMed:23733465). Upon phosphorylation by LytS,
CC functions as a transcription regulator by direct binding to promoter
CC regions of target genes including lrgA and lrgB, to positively regulate
CC their expression (PubMed:8824633, PubMed:25491472).
CC {ECO:0000269|PubMed:19502411, ECO:0000269|PubMed:23733465,
CC ECO:0000269|PubMed:25491472, ECO:0000269|PubMed:8824633}.
CC -!- SUBUNIT: Homodimer; when phosphorylated.
CC {ECO:0000250|UniProtKB:P60609}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated and dephosphorylated by LytS.
CC {ECO:0000269|PubMed:25491472}.
CC -!- DISRUPTION PHENOTYPE: Deletion significantly reduces target tissue
CC survival during calcium-daptomycin treatment and increases
CC susceptibility to host defense cationic antimicrobial peptides.
CC {ECO:0000269|PubMed:23733465}.
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DR EMBL; L42945; AAB48183.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29406.1; -; Genomic_DNA.
DR RefSeq; WP_000645452.1; NZ_LS483365.1.
DR RefSeq; YP_498826.1; NC_007795.1.
DR PDB; 6M8O; X-ray; 2.50 A; A=1-134.
DR PDBsum; 6M8O; -.
DR AlphaFoldDB; P60611; -.
DR SMR; P60611; -.
DR STRING; 1280.SAXN108_0241; -.
DR DNASU; 3920306; -.
DR EnsemblBacteria; ABD29406; ABD29406; SAOUHSC_00231.
DR GeneID; 3920306; -.
DR KEGG; sao:SAOUHSC_00231; -.
DR PATRIC; fig|93061.5.peg.212; -.
DR eggNOG; COG3279; Bacteria.
DR HOGENOM; CLU_000445_14_1_9; -.
DR OMA; DIHMPDF; -.
DR PRO; PR:P60611; -.
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:0001216; F:DNA-binding transcription activator activity; 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 transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR007492; LytTR_DNA-bd_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF04397; LytTR; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00850; LytTR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50930; HTH_LYTTR; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..246
FT /note="Transcriptional regulatory protein LytR"
FT /id="PRO_0000081131"
FT DOMAIN 2..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 141..245
FT /note="HTH LytTR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00112"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 53
FT /note="D->A: Complete loss of lrgAB promoter binding."
FT /evidence="ECO:0000269|PubMed:25491472"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6M8O"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:6M8O"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:6M8O"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:6M8O"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6M8O"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6M8O"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:6M8O"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6M8O"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:6M8O"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:6M8O"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:6M8O"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:6M8O"
SQ SEQUENCE 246 AA; 28221 MW; 4DC650CF75019F53 CRC64;
MKALIIDDEP LARNELTYLL NEIGGFEEIN EAENVKETLE ALLINQYDII FLDVNLMDEN
GIELGAKIQK MKEPPAIIFA TAHDQYAVQA FELNATDYIL KPFGQKRIEQ AVNKVRATKA
KDDNNASAIA NDMSANFDQS LPVEIDDKIH MLKQQNIIGI GTHNGITTIH TTNHKYETTE
PLNRYEKRLN PTYFIRIHRS YIINTKHIKE VQQWFNYTYM VILTNGVKMQ VGRSFMKDFK
ASIGLL
