ARLR_STAAR
ID ARLR_STAAR Reviewed; 219 AA.
AC Q6GGZ3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Response regulator ArlR;
GN Name=arlR; OrderedLocusNames=SAR1427;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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 ArlS/ArlR
CC involved in the regulation of adhesion, autolysis, multidrug resistance
CC and virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by ArlS. {ECO:0000250}.
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DR EMBL; BX571856; CAG40424.1; -; Genomic_DNA.
DR RefSeq; WP_000192137.1; NC_002952.2.
DR AlphaFoldDB; Q6GGZ3; -.
DR SMR; Q6GGZ3; -.
DR KEGG; sar:SAR1427; -.
DR HOGENOM; CLU_000445_30_1_9; -.
DR OMA; NIHGEGF; -.
DR OrthoDB; 1020672at2; -.
DR Proteomes; UP000000596; Chromosome.
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; Repressor;
KW Transcription; Transcription regulation; Two-component regulatory system;
KW Virulence.
FT CHAIN 1..219
FT /note="Response regulator ArlR"
FT /id="PRO_0000081017"
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"
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