ROT_STAAR
ID ROT_STAAR Reviewed; 166 AA.
AC Q6GFT9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=HTH-type transcriptional regulator rot;
DE AltName: Full=Repressor of toxins;
GN Name=rot; OrderedLocusNames=SAR1847;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Global regulator with both positive and negative effects that
CC mediates modulation of several genes involved in virulence. Also,
CC modulates the expression of genes not previously implicated in
CC pathogenesis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the rot family. {ECO:0000305}.
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DR EMBL; BX571856; CAG40838.1; -; Genomic_DNA.
DR PDB; 4Q77; X-ray; 1.77 A; A/B=34-166.
DR PDBsum; 4Q77; -.
DR AlphaFoldDB; Q6GFT9; -.
DR SMR; Q6GFT9; -.
DR KEGG; sar:SAR1847; -.
DR HOGENOM; CLU_132118_0_0_9; -.
DR OMA; LWDKGSM; -.
DR PRO; PR:Q6GFT9; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR016998; Rot.
DR InterPro; IPR010166; SarA/Rot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01047; MarR; 1.
DR PIRSF; PIRSF032474; TF_HTH_Rot; 1.
DR SMART; SM00347; HTH_MARR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR TIGRFAMs; TIGR01889; Staph_reg_Sar; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Repressor; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..166
FT /note="HTH-type transcriptional regulator rot"
FT /id="PRO_0000220547"
FT DNA_BIND 87..110
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT HELIX 41..66
FT /evidence="ECO:0007829|PDB:4Q77"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:4Q77"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4Q77"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:4Q77"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4Q77"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:4Q77"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:4Q77"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:4Q77"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4Q77"
FT HELIX 135..164
FT /evidence="ECO:0007829|PDB:4Q77"
SQ SEQUENCE 166 AA; 19417 MW; 71CF1F6D5B90571D CRC64;
MHKLAHISFG IVGMFVNTCM VAKYVIINWE MYSMKKVNND TVFGILQLET LLGDINSIFS
EIESEYKMSR EEILILLTLW QKGSMTLKEM DRFVEVKPYK RTRTYNNLVE LEWIYKERPV
DDERTVIIHF NEKLQQEKVE LLNFISDAIA SRATAMQNSL NAIIAV