SARR_STAA8
ID SARR_STAA8 Reviewed; 115 AA.
AC Q9F0R1; Q2G271;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=HTH-type transcriptional regulator SarR;
DE AltName: Full=Staphylococcal accessory regulator R;
GN Name=sarR; OrderedLocusNames=SAOUHSC_02566;
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], PROTEIN SEQUENCE OF 2-15, AND FUNCTION.
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 [2]
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 [3]
RP TRANSCRIPTION PROFILING.
RX PubMed=16237023; DOI=10.1128/jb.187.21.7397-7406.2005;
RA Senn M.M., Bischoff M., von Eiff C., Berger-Baechi B.;
RT "Sigma B activity in a Staphylococcus aureus hemB mutant.";
RL J. Bacteriol. 187:7397-7406(2005).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF ASP-6; ASP-9; LYS-19; LYS-25; LEU-38; LYS-52;
RP LYS-56; LYS-61; LYS-67; LEU-72; LYS-80; ARG-82; ASP-86; GLU-87; ARG-88;
RP GLN-98; LEU-105; GLU-108; GLU-110 AND GLU-111.
RX PubMed=16689803; DOI=10.1111/j.1365-2958.2006.05171.x;
RA Manna A.C., Cheung A.L.;
RT "Transcriptional regulation of the agr locus and the identification of DNA
RT binding residues of the global regulatory protein SarR in Staphylococcus
RT aureus.";
RL Mol. Microbiol. 60:1289-1301(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=11381122; DOI=10.1073/pnas.121013398;
RA Liu Y., Manna A.C., Li R., Martin W.E., Murphy R.C., Cheung A.L., Zhang G.;
RT "Crystal structure of the SarR protein from Staphylococcus aureus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6877-6882(2001).
CC -!- FUNCTION: Negative regulator of sarA transcription at late exponential
CC and stationary growth phases. It contributes to the modulation of
CC target genes downstream of the sarA regulatory cascade. Also,
CC positively regulates expression of primary transcripts RNAII and RNAIII
CC generated by agr (virulence accessory gene regulator) locus.
CC {ECO:0000269|PubMed:11159982, ECO:0000269|PubMed:16689803}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11381122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Maximally expressed at post-exponential growth phase. Level
CC of transcription reduced during exponential growth phase in hemB
CC (delta-aminolevulinic acid dehydratase) mutant.
CC -!- SIMILARITY: Belongs to the SarA family. {ECO:0000305}.
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DR EMBL; AF207701; AAG35715.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD31578.1; -; Genomic_DNA.
DR RefSeq; WP_000036076.1; NZ_LS483365.1.
DR RefSeq; YP_501027.1; NC_007795.1.
DR PDB; 1HSJ; X-ray; 2.30 A; A/B=1-115.
DR PDBsum; 1HSJ; -.
DR AlphaFoldDB; Q9F0R1; -.
DR SMR; Q9F0R1; -.
DR STRING; 1280.SAXN108_2543; -.
DR EnsemblBacteria; ABD31578; ABD31578; SAOUHSC_02566.
DR GeneID; 3921563; -.
DR KEGG; sao:SAOUHSC_02566; -.
DR PATRIC; fig|93061.5.peg.2315; -.
DR eggNOG; COG1846; Bacteria.
DR HOGENOM; CLU_164084_0_0_9; -.
DR OMA; HDERTVI; -.
DR EvolutionaryTrace; Q9F0R1; -.
DR PRO; PR:Q9F0R1; -.
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: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 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11159982"
FT CHAIN 2..115
FT /note="HTH-type transcriptional regulator SarR"
FT /id="PRO_0000219583"
FT DNA_BIND 51..74
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT MUTAGEN 6
FT /note="D->A: Reduces DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 9
FT /note="D->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 19
FT /note="K->A: Reduces DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 25
FT /note="K->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 38
FT /note="L->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 52
FT /note="K->A: Abolishes DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 56
FT /note="K->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 61
FT /note="K->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 67
FT /note="K->A: Reduces DNA binding to the agr promoter, but
FT abolishes DNA binding to the sarA promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 72
FT /note="L->G: Reduces DNA binding to the agr promoter, but
FT abolishes DNA binding to the sarA promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 80
FT /note="K->G: Abolishes DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 82
FT /note="R->A: Abolishes DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 86
FT /note="D->A: No effect on DNA binding to the agr promoter,
FT but reduces DNA binding to the sarA promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 87
FT /note="E->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 88
FT /note="R->A: Abolishes DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 98
FT /note="Q->A: Reduces DNA binding to both agr and sarA
FT promoters."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 105
FT /note="L->G: Abolishes DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 108
FT /note="E->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 110
FT /note="E->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT MUTAGEN 111
FT /note="E->A: No effect on DNA binding to the agr promoter."
FT /evidence="ECO:0000269|PubMed:16689803"
FT HELIX 7..24
FT /evidence="ECO:0007829|PDB:1HSJ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1HSJ"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:1HSJ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1HSJ"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1HSJ"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:1HSJ"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1HSJ"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1HSJ"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:1HSJ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1HSJ"
SQ SEQUENCE 115 AA; 13669 MW; D2CE40E2DB234DBD CRC64;
MSKINDINDL VNATFQVKKF FRDTKKKFNL NYEEIYILNH ILRSESNEIS SKEIAKCSEF
KPYYLTKALQ KLKDLKLLSK KRSLQDERTV IVYVTDTQKA NIQKLISELE EYIKN
