ADCR_STRP6
ID ADCR_STRP6 Reviewed; 147 AA.
AC Q5XEA3; P82546;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Transcriptional regulator AdcR;
GN Name=adcR; OrderedLocusNames=M6_Spy0125;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1] {ECO:0000312|EMBL:AAT86260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 7-18; 36-51; 60-70 AND 130-136, AND MASS SPECTROMETRY.
RC STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA VanBogelen R.A.;
RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT proteins.";
RL Submitted (MAY-2000) to UniProtKB.
CC -!- FUNCTION: Zinc-responsive regulator. {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Zinc acts as a coregulator and is required for
CC DNA-binding activity. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=16544.02; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.2};
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DR EMBL; CP000003; AAT86260.1; -; Genomic_DNA.
DR RefSeq; WP_002986587.1; NC_006086.1.
DR AlphaFoldDB; Q5XEA3; -.
DR SMR; Q5XEA3; -.
DR EnsemblBacteria; AAT86260; AAT86260; M6_Spy0125.
DR GeneID; 57851936; -.
DR KEGG; spa:M6_Spy0125; -.
DR HOGENOM; CLU_142321_1_0_9; -.
DR OMA; INATQAH; -.
DR PHI-base; PHI:3487; -.
DR Proteomes; UP000001167; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR000835; HTH_MarR-typ.
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; PS50995; HTH_MARR_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Metal-binding; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..147
FT /note="Transcriptional regulator AdcR"
FT /id="PRO_0000259405"
FT DOMAIN 1..143
FT /note="HTH marR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT DNA_BIND 54..77
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 147 AA; 16532 MW; 6C8ADA0FE9E0E35B CRC64;
MGTLEKKLDN LVNTILLKAE NQHELLFGAC QSDVKLTNTQ EHILMLLSQQ RLTNTDLAKA
LNISQAAVTK AIKSLVKQDM LAGTKDTVDA RVTYFELTEL AKPIASEHTH HHDETLNVYN
RLLQKFSAKE LEIVDKFVTV FAEELEG