SARA_STAAU
ID SARA_STAAU Reviewed; 124 AA.
AC P0C1U6; Q200K0; Q53600; Q53777;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Transcriptional regulator SarA;
DE AltName: Full=Staphylococcal accessory regulator A;
GN Name=sarA;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shawcross S.G., Edwards-Jones V., Dawson M.M., Foster H.A.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-113.
RC STRAIN=C101, C2, C437, C640, C720, D17, D22, D274, D365, D456, D470, D535,
RC D547, D97, EMRSA3, EMRSA4, EMRSA9, H116, H19, H295, H402, H417, H466, H512,
RC H560, H591, H707, H783, and H831;
RX PubMed=16622047; DOI=10.1099/mic.0.28620-0;
RA Cooper J.E., Feil E.J.;
RT "The phylogeny of Staphylococcus aureus -- which genes make the best intra-
RT species markers?";
RL Microbiology 152:1297-1305(2006).
RN [3]
RP SUBUNIT.
RC STRAIN=DB;
RX PubMed=10411747; DOI=10.1046/j.1365-2958.1999.01474.x;
RA Rechtin T.M., Gillaspy A.F., Schumacher M.A., Brennan R.G., Smeltzer M.S.,
RA Hurlburt B.K.;
RT "Characterization of the SarA virulence gene regulator of Staphylococcus
RT aureus.";
RL Mol. Microbiol. 33:307-316(1999).
RN [4]
RP STRAIN-DEPENDENT DIFFERENCES IN REGULATORY FUNCTION.
RC STRAIN=Various isolates;
RX PubMed=11796572; DOI=10.1128/iai.70.2.470-480.2002;
RA Blevins J.S., Beenken K.E., Elasri M.O., Hurlburt B.K., Smeltzer M.S.;
RT "Strain-dependent differences in the regulatory roles of sarA and agr in
RT Staphylococcus aureus.";
RL Infect. Immun. 70:470-480(2002).
RN [5]
RP FUNCTION IN BIOFILM DEVELOPMENT.
RC STRAIN=Isolate 15981;
RX PubMed=12753197; DOI=10.1046/j.1365-2958.2003.03493.x;
RA Valle J., Toledo-Arana A., Berasain C., Ghigo J.-M., Amorena B.,
RA Penades J.R., Lasa I.;
RT "SarA and not sigmaB is essential for biofilm development by Staphylococcus
RT aureus.";
RL Mol. Microbiol. 48:1075-1087(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Phillips;
RX PubMed=15822900; DOI=10.1021/pr049866k;
RA Nandakumar R., Nandakumar M.P., Marten M.R., Ross J.M.;
RT "Proteome analysis of membrane and cell wall associated proteins from
RT Staphylococcus aureus.";
RL J. Proteome Res. 4:250-257(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH DNA, AND SUBUNIT.
RC STRAIN=DB;
RX PubMed=11196648; DOI=10.1038/35051623;
RA Schumacher M.A., Hurlburt B.K., Brennan R.G.;
RT "Crystal structures of SarA, a pleiotropic regulator of virulence genes in
RT S. aureus.";
RL Nature 409:215-219(2001).
CC -!- FUNCTION: Global regulator with both positive and negative effects that
CC controls expression of several virulence factors and biofilm formation
CC process in a cell density-dependent manner. In a strain-dependent
CC manner plays a role in multidrug resistance mechanism. Is required for
CC transcription of primary transcripts RNAII and RNAIII generated by agr
CC (virulence accessory gene regulator) locus. Acts as a transcriptional
CC activator of the genes encoding, among others, for fibronectin binding
CC proteins (fnbA and fnbB), hemolysins (hla, hld, hlgB and hlgC), serine
CC proteases (splA, splB, splD and splF) and of the bap gene, which is
CC essential for biofilm development in some strains. Negatively regulates
CC the expression of the genes for protein A (spa), lipase (lip),
CC thermonuclease (nuc), immunodominant staphylococcal antigen B (isaB),
CC staphylococcal serine and cysteine proteases (sspA and sspB),
CC staphostatin B (sspC), metalloprotease aureolysin (aur) and collagen
CC adhesin (cna). Probably activates the development of biofilm by both
CC enhancing the ica operon transcription and suppressing the
CC transcription of either a protein involved in the turnover of PIA/PNAG
CC or a repressor of its synthesis, whose expression would be sigma-B-
CC dependent. {ECO:0000269|PubMed:12753197}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10411747,
CC ECO:0000269|PubMed:11196648}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Expressed at the exponential growth phase and maximally
CC induced during the transition from late exponential phase to stationary
CC phase. Repressed by SarR and activated by two-component regulatory
CC system ArlS/ArlR. Activated by SigB in strains harboring an intact sigB
CC operon (rsbU, rsbV, rsbW, and sigB). Transcription is also attenuated
CC by MsrR.
CC -!- MISCELLANEOUS: Can regulate transcription of some virulence factors
CC (hemolysins, staphylococcal serine and cysteine proteases, lipase,
CC protein A and metalloprotease aureolysin) via either agr-dependent
CC and/or agr-independent pathway. Agr and SarA have opposing effects on
CC the expression of sspA, sspB, sspC, lip and aur.
CC -!- SIMILARITY: Belongs to the SarA family. {ECO:0000305}.
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DR EMBL; AF515775; AAM74164.1; -; Genomic_DNA.
DR EMBL; DQ414117; ABD73686.1; -; Genomic_DNA.
DR EMBL; DQ414116; ABD73685.1; -; Genomic_DNA.
DR EMBL; DQ414115; ABD73684.1; -; Genomic_DNA.
DR EMBL; DQ414114; ABD73683.1; -; Genomic_DNA.
DR EMBL; DQ414113; ABD73682.1; -; Genomic_DNA.
DR EMBL; DQ414112; ABD73681.1; -; Genomic_DNA.
DR EMBL; DQ414111; ABD73680.1; -; Genomic_DNA.
DR EMBL; DQ414110; ABD73679.1; -; Genomic_DNA.
DR EMBL; DQ414109; ABD73678.1; -; Genomic_DNA.
DR EMBL; DQ414108; ABD73677.1; -; Genomic_DNA.
DR EMBL; DQ414107; ABD73676.1; -; Genomic_DNA.
DR EMBL; DQ414106; ABD73675.1; -; Genomic_DNA.
DR EMBL; DQ414105; ABD73674.1; -; Genomic_DNA.
DR EMBL; DQ414104; ABD73673.1; -; Genomic_DNA.
DR EMBL; DQ414103; ABD73672.1; -; Genomic_DNA.
DR EMBL; DQ414102; ABD73671.1; -; Genomic_DNA.
DR EMBL; DQ414101; ABD73670.1; -; Genomic_DNA.
DR EMBL; DQ414100; ABD73669.1; -; Genomic_DNA.
DR EMBL; DQ414099; ABD73668.1; -; Genomic_DNA.
DR EMBL; DQ414098; ABD73667.1; -; Genomic_DNA.
DR EMBL; DQ414097; ABD73666.1; -; Genomic_DNA.
DR EMBL; DQ414096; ABD73665.1; -; Genomic_DNA.
DR EMBL; DQ414095; ABD73664.1; -; Genomic_DNA.
DR EMBL; DQ414094; ABD73663.1; -; Genomic_DNA.
DR EMBL; DQ414093; ABD73662.1; -; Genomic_DNA.
DR EMBL; DQ414092; ABD73661.1; -; Genomic_DNA.
DR EMBL; DQ414091; ABD73660.1; -; Genomic_DNA.
DR EMBL; DQ414090; ABD73659.1; -; Genomic_DNA.
DR EMBL; DQ414089; ABD73658.1; -; Genomic_DNA.
DR RefSeq; WP_001018677.1; NZ_WYDB01000005.1.
DR AlphaFoldDB; P0C1U6; -.
DR SMR; P0C1U6; -.
DR OMA; AMITYAD; -.
DR EvolutionaryTrace; P0C1U6; -.
DR PHI-base; PHI:3305; -.
DR PRO; PR:P0C1U6; -.
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 GO; GO:0090609; P:single-species submerged biofilm formation; IMP:CACAO.
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; 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_0000219576"
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
