MGRA_STAAU
ID MGRA_STAAU Reviewed; 147 AA.
AC P0C1S0; Q7X448; Q83ZI4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=HTH-type transcriptional regulator MgrA;
DE AltName: Full=Regulator of autolytic activity;
GN Name=mgrA; Synonyms=mgr;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Becker;
RX PubMed=12813062; DOI=10.1128/jb.185.13.3703-3710.2003;
RA Luong T.T., Newell S.W., Lee C.Y.;
RT "Mgr, a novel global regulator in Staphylococcus aureus.";
RL J. Bacteriol. 185:3703-3710(2003).
CC -!- FUNCTION: Regulatory protein involved in autolytic activity, multidrug
CC resistance and virulence (By similarity). Negatively controls spa
CC (surface protein A) transcription. Activates type 8 capsular
CC polysaccharide (cap8) and nuclease (nuc) biosynthesis. Represses
CC coagulase and protease production. {ECO:0000250,
CC ECO:0000269|PubMed:12813062}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: In strain Becker, gene disruption may lead to increase
CC in alpha-hemolysin (hla).
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DR EMBL; AY293568; AAP48794.1; -; Genomic_DNA.
DR RefSeq; WP_001283444.1; NZ_WYDB01000004.1.
DR PDB; 2BV6; X-ray; 2.80 A; A=6-143.
DR PDBsum; 2BV6; -.
DR AlphaFoldDB; P0C1S0; -.
DR SMR; P0C1S0; -.
DR BindingDB; P0C1S0; -.
DR ChEMBL; CHEMBL2331056; -.
DR GeneID; 66838978; -.
DR OMA; AHRMTKS; -.
DR EvolutionaryTrace; P0C1S0; -.
DR PHI-base; PHI:3058; -.
DR PHI-base; PHI:6255; -.
DR PRO; PR:P0C1S0; -.
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 Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR023187; Tscrpt_reg_MarR-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01047; MarR; 1.
DR SMART; SM00347; HTH_MARR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS01117; HTH_MARR_1; 1.
DR PROSITE; PS50995; HTH_MARR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Repressor; Transcription;
KW Transcription regulation; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..147
FT /note="HTH-type transcriptional regulator MgrA"
FT /id="PRO_0000054366"
FT DOMAIN 8..139
FT /note="HTH marR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT DNA_BIND 55..78
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT HELIX 11..29
FT /evidence="ECO:0007829|PDB:2BV6"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:2BV6"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:2BV6"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:2BV6"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:2BV6"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2BV6"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:2BV6"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2BV6"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2BV6"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2BV6"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:2BV6"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:2BV6"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:2BV6"
SQ SEQUENCE 147 AA; 17089 MW; F5EA62A451EF9FC8 CRC64;
MSDQHNLKEQ LCFSLYNAQR QVNRYYSNKV FKKYNLTYPQ FLVLTILWDE SPVNVKKVVT
ELALDTGTVS PLLKRMEQVD LIKRERSEVD QREVFIHLTD KSETIRPELS NASDKVASAS
SLSQDEVKEL NRLLGKVIHA FDETKEK