ARLR_STAA8
ID ARLR_STAA8 Reviewed; 219 AA.
AC Q9KJN4; Q2FYL9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Response regulator ArlR;
GN Name=arlR; OrderedLocusNames=SAOUHSC_01420;
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], AND FUNCTION.
RX PubMed=10869073; DOI=10.1128/jb.182.14.3955-3964.2000;
RA Fournier B., Hooper D.C.;
RT "A new two-component regulatory system involved in adhesion, autolysis, and
RT extracellular proteolytic activity of Staphylococcus aureus.";
RL J. Bacteriol. 182:3955-3964(2000).
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.
RX PubMed=10633099; DOI=10.1128/jb.182.3.664-671.2000;
RA Fournier B., Aras R., Hooper D.C.;
RT "Expression of the multidrug resistance transporter NorA from
RT Staphylococcus aureus is modified by a two-component regulatory system.";
RL J. Bacteriol. 182:664-671(2000).
RN [4]
RP FUNCTION, AND REGULATION.
RX PubMed=11454217; DOI=10.1046/j.1365-2958.2001.02515.x;
RA Fournier B., Klier A., Rapoport G.;
RT "The two-component system ArlS-ArlR is a regulator of virulence gene
RT expression in Staphylococcus aureus.";
RL Mol. Microbiol. 41:247-261(2001).
RN [5]
RP REGULATION BY MGRA.
RX PubMed=12791130; DOI=10.1046/j.1365-2958.2003.03503.x;
RA Ingavale S.S., Van Wamel W., Cheung A.L.;
RT "Characterization of RAT, an autolysis regulator in Staphylococcus
RT aureus.";
RL Mol. Microbiol. 48:1451-1466(2003).
RN [6]
RP REGULATION BY SARV.
RX PubMed=15292128; DOI=10.1128/jb.186.16.5267-5280.2004;
RA Manna A.C., Ingavale S.S., Maloney M., van Wamel W., Cheung A.L.;
RT "Identification of sarV (SA2062), a new transcriptional regulator, is
RT repressed by SarA and MgrA (SA0641) and involved in the regulation of
RT autolysis in Staphylococcus aureus.";
RL J. Bacteriol. 186:5267-5280(2004).
RN [7]
RP FUNCTION.
RX PubMed=15528666; DOI=10.1099/mic.0.27194-0;
RA Fournier B., Klier A.;
RT "Protein A gene expression is regulated by DNA supercoiling which is
RT modified by the ArlS-ArlR two-component system of Staphylococcus aureus.";
RL Microbiology 150:3807-3819(2004).
RN [8]
RP FUNCTION IN BIOFILM DEVELOPMENT.
RX PubMed=16030226; DOI=10.1128/jb.187.15.5318-5329.2005;
RA Toledo-Arana A., Merino N., Vergara-Irigaray M., Debarbouille M.,
RA Penades J.R., Lasa I.;
RT "Staphylococcus aureus develops an alternative, ica-independent biofilm in
RT the absence of the arlRS two-component system.";
RL J. Bacteriol. 187:5318-5329(2005).
CC -!- FUNCTION: Member of the two-component regulatory system ArlS/ArlR
CC involved in the regulation of adhesion, autolysis, multidrug resistance
CC and virulence. ArlS/ArlR affects expression of the multidrug resistance
CC transporter NorA and interacts with both Agr (virulence accessory gene
CC regulator) (negatively) and SarA (staphylococcal accessory regulator)
CC (positively) to modulate several virulence factor genes, including ssp
CC (serine protease), spa (surface protein A) and hla (alpha-hemolysin).
CC Could inhibit biofilm development by a mechanism independent of the
CC presence of the poly-N-acetylglucosamine (PNAG). Also, Arl proteins are
CC required for the efficient activity of DNA gyrase inhibitors and high
CC osmolarity on spa expression. {ECO:0000269|PubMed:10633099,
CC ECO:0000269|PubMed:10869073, ECO:0000269|PubMed:11454217,
CC ECO:0000269|PubMed:15528666, ECO:0000269|PubMed:16030226}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Activated by Agr, SarA, SarV and MgrA.
CC -!- PTM: Phosphorylated by ArlS. {ECO:0000305}.
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DR EMBL; AF165314; AAF85896.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30513.1; -; Genomic_DNA.
DR RefSeq; WP_000192137.1; NZ_LS483365.1.
DR RefSeq; YP_499946.1; NC_007795.1.
DR PDB; 6IJU; X-ray; 2.40 A; A=123-219.
DR PDB; 6IS1; X-ray; 1.59 A; A/B/C/D/E/F/G/H=2-121.
DR PDB; 6IS2; X-ray; 1.59 A; A/B/C/D=2-121.
DR PDB; 6IS3; X-ray; 1.55 A; A/C=2-119.
DR PDB; 6IS4; X-ray; 1.85 A; A=123-219.
DR PDB; 6KYX; X-ray; 2.00 A; A=122-219.
DR PDBsum; 6IJU; -.
DR PDBsum; 6IS1; -.
DR PDBsum; 6IS2; -.
DR PDBsum; 6IS3; -.
DR PDBsum; 6IS4; -.
DR PDBsum; 6KYX; -.
DR AlphaFoldDB; Q9KJN4; -.
DR SMR; Q9KJN4; -.
DR STRING; 1280.SAXN108_1434; -.
DR EnsemblBacteria; ABD30513; ABD30513; SAOUHSC_01420.
DR GeneID; 3920651; -.
DR KEGG; sao:SAOUHSC_01420; -.
DR PATRIC; fig|93061.5.peg.1299; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_1_9; -.
DR OMA; NIHGEGF; -.
DR PRO; PR:Q9KJN4; -.
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 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 Reference proteome; Repressor; Transcription; Transcription regulation;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..219
FT /note="Response regulator ArlR"
FT /id="PRO_0000081013"
FT DOMAIN 3..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 122..219
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6KYX"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6KYX"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6KYX"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:6KYX"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:6KYX"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6KYX"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:6KYX"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:6KYX"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:6KYX"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6KYX"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:6KYX"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6KYX"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6KYX"
SQ SEQUENCE 219 AA; 25498 MW; 721458C704EBFDF7 CRC64;
MTQILIVEDE QNLARFLELE LTHENYNVDT EYDGQDGLDK ALSHYYDLII LDLMLPSING
LEICRKIRQQ QSTPIIIITA KSDTYDKVAG LDYGADDYIV KPFDIEELLA RIRAILRRQP
QKDIIDVNGI TIDKNAFKVT VNGAEIELTK TEYDLLYLLA ENKNHVMQRE QILNHVWGYN
SEVETNVVDV YIRYLRNKLK PYDRDKMIET VRGVGYVIR
