SARA_STAAC
ID SARA_STAAC Reviewed; 124 AA.
AC Q5HI51;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Transcriptional regulator SarA;
DE AltName: Full=Staphylococcal accessory regulator A;
GN Name=sarA; OrderedLocusNames=SACOL0672;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-17, AND REGULATION BY SIGB.
RX PubMed=11092859; DOI=10.1128/jb.182.24.6983-6991.2000;
RA Gertz S., Engelmann S., Schmid R., Ziebandt A.-K., Tischer K., Scharf C.,
RA Hacker J., Hecker M.;
RT "Characterization of the sigma(B) regulon in Staphylococcus aureus.";
RL J. Bacteriol. 182:6983-6991(2000).
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 -!- INDUCTION: Activated by SigB.
CC -!- SIMILARITY: Belongs to the SarA family. {ECO:0000305}.
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DR EMBL; CP000046; AAW36362.1; -; Genomic_DNA.
DR RefSeq; WP_001018677.1; NC_002951.2.
DR AlphaFoldDB; Q5HI51; -.
DR SMR; Q5HI51; -.
DR EnsemblBacteria; AAW36362; AAW36362; SACOL0672.
DR KEGG; sac:SACOL0672; -.
DR HOGENOM; CLU_164084_0_0_9; -.
DR OMA; AMITYAD; -.
DR PRO; PR:Q5HI51; -.
DR Proteomes; UP000000530; Chromosome.
DR CollecTF; EXPREG_00000ef0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IPI:CollecTF.
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 1: Evidence at protein level;
KW Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Metal-binding; Repressor; Transcription; Transcription regulation;
KW Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11092859"
FT CHAIN 2..124
FT /note="Transcriptional regulator SarA"
FT /id="PRO_0000219577"
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