SARS_STAA8
ID SARS_STAA8 Reviewed; 250 AA.
AC Q2G1N7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=HTH-type transcriptional regulator SarS;
DE AltName: Full=Staphylococcal accessory regulator S;
GN Name=sarS; Synonyms=sarH1; OrderedLocusNames=SAOUHSC_00070;
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 [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 [2]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, AND GROWTH PHASE-DEPENDENT EXPRESSION.
RX PubMed=10931334; DOI=10.1046/j.1365-2958.2000.02003.x;
RA Tegmark K., Karlsson A., Arvidson S.;
RT "Identification and characterization of SarH1, a new global regulator of
RT virulence gene expression in Staphylococcus aureus.";
RL Mol. Microbiol. 37:398-409(2000).
RN [3]
RP FUNCTION.
RX PubMed=11254606; DOI=10.1128/iai.69.4.2448-2455.2001;
RA Cheung A.L., Schmidt K.A., Bateman B., Manna A.C.;
RT "SarS, a SarA homolog repressible by agr, is an activator of protein A
RT synthesis in Staphylococcus aureus.";
RL Infect. Immun. 69:2448-2455(2001).
RN [4]
RP REGULATION BY SART.
RX PubMed=12933857; DOI=10.1128/iai.71.9.5139-5148.2003;
RA Schmidt K.A., Manna A.C., Cheung A.L.;
RT "SarT influences sarS expression in Staphylococcus aureus.";
RL Infect. Immun. 71:5139-5148(2003).
RN [5]
RP REGULATION BY ROT.
RX PubMed=12511508; DOI=10.1128/jb.185.2.610-619.2003;
RA Said-Salim B., Dunman P.M., McAleese F.M., Macapagal D., Murphy E.,
RA McNamara P.J., Arvidson S., Foster T.J., Projan S.J., Kreiswirth B.N.;
RT "Global regulation of Staphylococcus aureus genes by Rot.";
RL J. Bacteriol. 185:610-619(2003).
RN [6]
RP STRAIN-DEPENDENT DIFFERENCES IN REGULATION BY TCAR.
RX PubMed=15126456; DOI=10.1128/jb.186.10.2966-2972.2004;
RA McCallum N., Bischoff M., Maki H., Wada A., Berger-Baechi B.;
RT "TcaR, a putative MarR-like regulator of sarS expression.";
RL J. Bacteriol. 186:2966-2972(2004).
RN [7]
RP MODEL FOR SPA PROMOTER REGULATION.
RX PubMed=15175287; DOI=10.1128/jb.186.12.3738-3748.2004;
RA Gao J., Stewart G.C.;
RT "Regulatory elements of the Staphylococcus aureus protein A (Spa)
RT promoter.";
RL J. Bacteriol. 186:3738-3748(2004).
RN [8]
RP REGULATION BY MGRA.
RX PubMed=15731040; DOI=10.1128/iai.73.3.1423-1431.2005;
RA Ingavale S.S., van Wamel W., Luong T.T., Lee C.Y., Cheung A.L.;
RT "Rat/MgrA, a regulator of autolysis, is a regulator of virulence genes in
RT Staphylococcus aureus.";
RL Infect. Immun. 73:1423-1431(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND OVERVIEW OF SARS AND SPA
RP REGULATION.
RX PubMed=16128400; DOI=10.1016/j.ijmm.2005.05.003;
RA Oscarsson J., Harlos C., Arvidson S.;
RT "Regulatory role of proteins binding to the spa (protein A) and sarS
RT (staphylococcal accessory regulator) promoter regions in Staphylococcus
RT aureus NTCC 8325-4.";
RL Int. J. Med. Microbiol. 295:253-266(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=12837797; DOI=10.1128/jb.185.14.4219-4225.2003;
RA Li R., Manna A.C., Dai S., Cheung A.L., Zhang G.;
RT "Crystal structure of the SarS protein from Staphylococcus aureus.";
RL J. Bacteriol. 185:4219-4225(2003).
CC -!- FUNCTION: Transcriptional regulator that controls expression of some
CC virulence factors in a cell density-dependent manner. Acts as an
CC activator of the gene encoding protein A (spa). Negatively regulates
CC the expression of alpha-hemolysin (hla). {ECO:0000269|PubMed:10931334,
CC ECO:0000269|PubMed:11254606}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Expressed at the early exponential growth phase, decreases
CC through exponential phase and reaches a steady-state level at post-
CC exponential phase. Repressed by MgrA and SarA. Activated by Rot and
CC SarT. Transcription is also dependent on SigA and SigB factors. Is
CC activated by SigB in strains harboring an intact sigB operon (rsbU,
CC rsbV, rsbW, and sigB).
CC -!- MISCELLANEOUS: Mutational analysis of the spa promoter suggests that
CC SarS might stimulate spa transcription by competing with SarA.
CC -!- MISCELLANEOUS: The regulatory events observed in strain NCTC 8325 are
CC not representative of the events that occur in clinical isolates of
CC S.aureus.
CC -!- SIMILARITY: Belongs to the SarA family. {ECO:0000305}.
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DR EMBL; CP000253; ABD29254.1; -; Genomic_DNA.
DR RefSeq; WP_000876756.1; NZ_LS483365.1.
DR RefSeq; YP_498671.1; NC_007795.1.
DR PDB; 1P4X; X-ray; 2.20 A; A=1-250.
DR PDBsum; 1P4X; -.
DR AlphaFoldDB; Q2G1N7; -.
DR SMR; Q2G1N7; -.
DR STRING; 1280.SAXN108_0097; -.
DR EnsemblBacteria; ABD29254; ABD29254; SAOUHSC_00070.
DR GeneID; 3919449; -.
DR KEGG; sao:SAOUHSC_00070; -.
DR PATRIC; fig|93061.5.peg.60; -.
DR eggNOG; COG1846; Bacteria.
DR HOGENOM; CLU_097164_0_0_9; -.
DR OMA; DHIIKQF; -.
DR EvolutionaryTrace; Q2G1N7; -.
DR PRO; PR:Q2G1N7; -.
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:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR010166; SarA/Rot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR SMART; SM00347; HTH_MARR; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR TIGRFAMs; TIGR01889; Staph_reg_Sar; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..250
FT /note="HTH-type transcriptional regulator SarS"
FT /id="PRO_0000249329"
FT DNA_BIND 53..76
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT DNA_BIND 177..200
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT HELIX 8..26
FT /evidence="ECO:0007829|PDB:1P4X"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 98..121
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 133..153
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:1P4X"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 222..238
FT /evidence="ECO:0007829|PDB:1P4X"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1P4X"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1P4X"
SQ SEQUENCE 250 AA; 29890 MW; 4680D50FE86DDC19 CRC64;
MKYNNHDKIR DFIIIEAYMF RFKKKVKPEV DMTIKEFILL TYLFHQQENT LPFKKIVSDL
CYKQSDLVQH IKVLVKHSYI SKVRSKIDER NTYISISEEQ REKIAERVTL FDQIIKQFNL
ADQSESQMIP KDSKEFLNLM MYTMYFKNII KKHLTLSFVE FTILAIITSQ NKNIVLLKDL
IETIHHKYPQ TVRALNNLKK QGYLIKERST EDERKILIHM DDAQQDHAEQ LLAQVNQLLA
DKDHLHLVFE
