SARA_STAAW
ID SARA_STAAW Reviewed; 124 AA.
AC Q7A1N5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Transcriptional regulator SarA;
DE AltName: Full=Staphylococcal accessory regulator A;
GN Name=sarA; OrderedLocusNames=MW0580;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT, FUNCTION, AND MUTAGENESIS
RP OF ASP-8; CYS-9; GLU-11; TYR-18; LYS-21; LYS-23; LYS-28; GLU-29; GLU-36;
RP LYS-54; LYS-69; LEU-74; PHE-80; LYS-82; ARG-84; ASP-88; GLU-89 AND ARG-90.
RX PubMed=16455801; DOI=10.1073/pnas.0510439103;
RA Liu Y., Manna A.C., Pan C.-H., Kriksunov I.A., Thiel D.J., Cheung A.L.,
RA Zhang G.;
RT "Structural and function analyses of the global regulatory protein SarA
RT from Staphylococcus aureus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2392-2397(2006).
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 (By similarity).
CC Required for transcription of primary transcripts RNAII and RNAIII
CC generated by agr (virulence accessory gene regulator) locus. Negatively
CC regulates the expression of spa (protein A) and aur (metalloprotease
CC aureolysin). {ECO:0000250, ECO:0000269|PubMed:16455801}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16455801}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SarA family. {ECO:0000305}.
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DR EMBL; BA000033; BAB94445.1; -; Genomic_DNA.
DR RefSeq; WP_001018677.1; NC_003923.1.
DR PDB; 2FNP; X-ray; 2.60 A; A/B=1-124.
DR PDB; 2FRH; X-ray; 2.50 A; A/B=2-124.
DR PDBsum; 2FNP; -.
DR PDBsum; 2FRH; -.
DR AlphaFoldDB; Q7A1N5; -.
DR SMR; Q7A1N5; -.
DR DIP; DIP-61104N; -.
DR EnsemblBacteria; BAB94445; BAB94445; BAB94445.
DR KEGG; sam:MW0580; -.
DR HOGENOM; CLU_164084_0_0_9; -.
DR OMA; AMITYAD; -.
DR EvolutionaryTrace; Q7A1N5; -.
DR PHI-base; PHI:6477; -.
DR PRO; PR:Q7A1N5; -.
DR Proteomes; UP000000418; 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; 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 3D-structure; Activator; Cytoplasm; DNA-binding; Metal-binding; Repressor;
KW 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_0000219582"
FT BINDING 7
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 11
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT MUTAGEN 8
FT /note="D->A: Able to bind to the agr promoter, but fails to
FT repress spa expression or to activate RNAII transcription;
FT when associated with A-11."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 9
FT /note="C->A: Reduced binding to the spa promoter. Fails to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 11
FT /note="E->A: Able to bind to the agr promoter, but fails to
FT repress spa expression or to activate RNAII transcription;
FT when associated with A-8."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 18
FT /note="Y->A: Reduced binding to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 21
FT /note="K->A: Able to bind to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 23
FT /note="K->A: Able to bind to the spa promoter. Fails to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 28
FT /note="K->A: Able to bind to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 29
FT /note="E->A: Reduced binding to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 36
FT /note="E->A: Reduced binding to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 54
FT /note="K->A: Reduced binding to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 69
FT /note="K->A: Able to bind to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 74
FT /note="L->A: Reduced binding to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 80
FT /note="F->A: Reduced binding to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 82
FT /note="K->A: Able to bind to the spa promoter. Able to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 84
FT /note="R->A: Unable to bind to the spa promoter. Fails to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 88
FT /note="D->A: Able to bind to the spa promoter. Fails to
FT repress spa and aur expression."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 89
FT /note="E->A: Able to bind to the spa promoter. Unable to
FT bind to the spa promoter; when associated with A-90. Fails
FT to repress spa and aur expression; even when associated
FT with A-90."
FT /evidence="ECO:0000269|PubMed:16455801"
FT MUTAGEN 90
FT /note="R->A: Unable to bind to the spa promoter; even when
FT associated with A-89. Fails to repress spa and aur
FT expression; even when associated with A-89."
FT /evidence="ECO:0000269|PubMed:16455801"
FT HELIX 9..28
FT /evidence="ECO:0007829|PDB:2FRH"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:2FRH"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2FRH"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:2FRH"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2FRH"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:2FRH"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:2FNP"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2FRH"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2FRH"
FT HELIX 99..121
FT /evidence="ECO:0007829|PDB:2FRH"
SQ SEQUENCE 124 AA; 14718 MW; DB9A16E806C10661 CRC64;
MAITKINDCF ELLSMVTYAD KLKSLIKKEF SISFEEFAVL TYISENKEKE YYLKDIINHL
NYKQPQVVKA VKILSQEDYF DKKRNEHDER TVLILVNAQQ RKKIESLLSR VNKRITEANN
EIEL
