SARA_STAA8
ID SARA_STAA8 Reviewed; 124 AA.
AC Q2G2U9; Q53600; Q53777;
DT 05-SEP-2006, 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=SAOUHSC_00620;
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].
RX PubMed=8021198; DOI=10.1128/jb.176.13.4168-4172.1994;
RA Cheung A.L., Projan S.J.;
RT "Cloning and sequencing of sarA of Staphylococcus aureus, a gene required
RT for the expression of agr.";
RL J. Bacteriol. 176:4168-4172(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8755885; DOI=10.1128/jb.178.15.4563-4570.1996;
RA Bayer M.G., Heinrichs J.H., Cheung A.L.;
RT "The molecular architecture of the sar locus in Staphylococcus aureus.";
RL J. Bacteriol. 178:4563-4570(1996).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=9446568; DOI=10.1074/jbc.273.5.2645;
RA Chien Y., Cheung A.L.;
RT "Molecular interactions between two global regulators, sar and agr, in
RT Staphylococcus aureus.";
RL J. Biol. Chem. 273:2645-2652(1998).
RN [5]
RP FUNCTION, AND GROWTH PHASE-DEPENDENT EXPRESSION.
RX PubMed=10411748; DOI=10.1046/j.1365-2958.1999.01475.x;
RA Blevins J.S., Gillaspy A.F., Rechtin T.M., Hurlburt B.K., Smeltzer M.S.;
RT "The Staphylococcal accessory regulator (sar) represses transcription of
RT the Staphylococcus aureus collagen adhesin gene (cna) in an agr-independent
RT manner.";
RL Mol. Microbiol. 33:317-326(1999).
RN [6]
RP REGULATION BY SARR.
RX PubMed=11159982; DOI=10.1128/iai.69.2.885-896.2001;
RA Manna A.C., Cheung A.L.;
RT "Characterization of sarR, a modulator of sar expression in Staphylococcus
RT aureus.";
RL Infect. Immun. 69:885-896(2001).
RN [7]
RP REGULATION BY SIGB.
RX PubMed=11489871; DOI=10.1128/jb.183.17.5171-5179.2001;
RA Bischoff M., Entenza J.M., Giachino P.;
RT "Influence of a functional sigB operon on the global regulators sar and agr
RT in Staphylococcus aureus.";
RL J. Bacteriol. 183:5171-5179(2001).
RN [8]
RP TRANSCRIPTION PROFILING.
RX PubMed=11717293; DOI=10.1128/jb.183.24.7341-7353.2001;
RA Dunman P.M., Murphy E., Haney S., Palacios D., Tucker-Kellogg G., Wu S.,
RA Brown E.L., Zagursky R.J., Shlaes D., Projan S.J.;
RT "Transcription profiling-based identification of Staphylococcus aureus
RT genes regulated by the agr and/or sarA loci.";
RL J. Bacteriol. 183:7341-7353(2001).
RN [9]
RP REGULATION BY ARLS/ARLR.
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 [10]
RP STRAIN-DEPENDENT DIFFERENCES IN REGULATORY FUNCTION.
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 [11]
RP REGULATION BY MSRR.
RX PubMed=12878519; DOI=10.1128/aac.47.8.2558-2564.2003;
RA Rossi J., Bischoff M., Wada A., Berger-Baechi B.;
RT "MsrR, a putative cell envelope-associated element involved in
RT Staphylococcus aureus sarA attenuation.";
RL Antimicrob. Agents Chemother. 47:2558-2564(2003).
RN [12]
RP FUNCTION IN BIOFILM DEVELOPMENT.
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 [13]
RP FUNCTION IN INTRINSIC MULTIDRUG RESISTANCE MECHANISM.
RX PubMed=15321676; DOI=10.1111/j.1574-6968.2004.tb09710.x;
RA O'Leary J.O., Langevin M.J., Price C.T., Blevins J.S., Smeltzer M.S.,
RA Gustafson J.E.;
RT "Effects of sarA inactivation on the intrinsic multidrug resistance
RT mechanism of Staphylococcus aureus.";
RL FEMS Microbiol. Lett. 237:297-302(2004).
RN [14]
RP FUNCTION.
RX PubMed=14702415; DOI=10.1099/mic.0.26634-0;
RA Shaw L., Golonka E., Potempa J., Foster S.J.;
RT "The role and regulation of the extracellular proteases of Staphylococcus
RT aureus.";
RL Microbiology 150:217-228(2004).
RN [15]
RP FUNCTION.
RX PubMed=16077127; DOI=10.1128/jb.187.16.5790-5798.2005;
RA Trotonda M.P., Manna A.C., Cheung A.L., Lasa I., Penades J.R.;
RT "SarA positively controls bap-dependent biofilm formation in Staphylococcus
RT aureus.";
RL J. Bacteriol. 187:5790-5798(2005).
RN [16]
RP EFFECT ON PLANT INFECTION MODEL.
RX PubMed=15842626; DOI=10.1111/j.1365-313x.2005.02385.x;
RA Prithiviraj B., Bais H.P., Jha A.K., Vivanco J.M.;
RT "Staphylococcus aureus pathogenicity on Arabidopsis thaliana is mediated
RT either by a direct effect of salicylic acid on the pathogen or by SA-
RT dependent, NPR1-independent host responses.";
RL Plant J. 42:417-432(2005).
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:10411748, ECO:0000269|PubMed:12753197,
CC ECO:0000269|PubMed:14702415, ECO:0000269|PubMed:15321676,
CC ECO:0000269|PubMed:16077127, ECO:0000269|PubMed:9446568}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 -!- MISCELLANEOUS: The 11 C-terminal amino acids are absent in substrain
CC NCTC 8325 / RN6390 (AAB05396) due to a nonsense mutation (UGA).
CC However, this truncated SarA protein is functional.
CC -!- MISCELLANEOUS: The regulatory events observed in strain NCTC 8325 /
CC RN6390 are not representative of the events that occur in clinical
CC isolates of S.aureus.
CC -!- MISCELLANEOUS: Strains NCTC 8325 and NCTC 8325 / RN6390 are able to
CC infect and kill Arabidopsis thaliana. This effect is attenuated in sarA
CC and agr mutant backgrounds.
CC -!- SIMILARITY: Belongs to the SarA family. {ECO:0000305}.
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DR EMBL; U20782; AAA62477.1; -; Genomic_DNA.
DR EMBL; U46541; AAB05396.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29758.1; -; Genomic_DNA.
DR RefSeq; WP_001018677.1; NZ_LS483365.1.
DR RefSeq; YP_499183.1; NC_007795.1.
DR AlphaFoldDB; Q2G2U9; -.
DR SMR; Q2G2U9; -.
DR STRING; 1280.SAXN108_0683; -.
DR EnsemblBacteria; ABD29758; ABD29758; SAOUHSC_00620.
DR GeneID; 3918939; -.
DR KEGG; sao:SAOUHSC_00620; -.
DR PATRIC; fig|93061.5.peg.556; -.
DR eggNOG; COG1846; Bacteria.
DR HOGENOM; CLU_164084_0_0_9; -.
DR OMA; AMITYAD; -.
DR PRO; PR:Q2G2U9; -.
DR Proteomes; UP000008816; 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; IBA:GO_Central.
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; Reference proteome;
KW Repressor; Transcription; 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_0000249323"
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"
FT CONFLICT 53
FT /note="L -> F (in Ref. 2; AAB05396)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..124
FT /note="Missing (in Ref. 2; AAB05396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 14718 MW; DB9A16E806C10661 CRC64;
MAITKINDCF ELLSMVTYAD KLKSLIKKEF SISFEEFAVL TYISENKEKE YYLKDIINHL
NYKQPQVVKA VKILSQEDYF DKKRNEHDER TVLILVNAQQ RKKIESLLSR VNKRITEANN
EIEL
