ID   SARA_STAAR              Reviewed;         124 AA.
AC   Q6GJ52;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Transcriptional regulator SarA;
DE   AltName: Full=Staphylococcal accessory regulator A;
GN   Name=sarA; OrderedLocusNames=SAR0625;
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: Global regulator with both positive and negative effects that
CC       controls the expression of several virulence factors and the biofilm
CC       formation process in a cell density-dependent manner. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SarA family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG39643.1; -; Genomic_DNA.
DR   RefSeq; WP_001018677.1; NC_002952.2.
DR   AlphaFoldDB; Q6GJ52; -.
DR   SMR; Q6GJ52; -.
DR   KEGG; sar:SAR0625; -.
DR   HOGENOM; CLU_164084_0_0_9; -.
DR   OMA; AMITYAD; -.
DR   OrthoDB; 1689031at2; -.
DR   PRO; PR:Q6GJ52; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR010166; SarA/Rot.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   TIGRFAMs; TIGR01889; Staph_reg_Sar; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Repressor; Transcription;
KW   Transcription regulation; Virulence.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..124
FT                   /note="Transcriptional regulator SarA"
FT                   /id="PRO_0000219580"
FT   BINDING         7
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         8
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  14718 MW;  DB9A16E806C10661 CRC64;
     MAITKINDCF ELLSMVTYAD KLKSLIKKEF SISFEEFAVL TYISENKEKE YYLKDIINHL
     NYKQPQVVKA VKILSQEDYF DKKRNEHDER TVLILVNAQQ RKKIESLLSR VNKRITEANN
     EIEL