ADCR_STRP2
ID ADCR_STRP2 Reviewed; 146 AA.
AC Q04I02;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Transcriptional regulator AdcR;
GN Name=adcR; OrderedLocusNames=SPD_2000;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [2]
RP FUNCTION, DNA-BINDING, REGULATION, SUBUNIT, ZINC-BINDING, AND MUTAGENESIS
RP OF CYS-30; HIS-42; HIS-108; HIS-111 AND HIS-112.
RC STRAIN=D39 / NCTC 7466;
RX PubMed=20804771; DOI=10.1016/j.jmb.2010.08.030;
RA Reyes-Caballero H., Guerra A.J., Jacobsen F.E., Kazmierczak K.M.,
RA Cowart D., Koppolu U.M., Scott R.A., Winkler M.E., Giedroc D.P.;
RT "The metalloregulatory zinc site in Streptococcus pneumoniae AdcR, a zinc-
RT activated MarR family repressor.";
RL J. Mol. Biol. 403:197-216(2010).
RN [3]
RP FUNCTION, DNA-BINDING, AND REGULATION.
RC STRAIN=D39 / NCTC 7466;
RX PubMed=21603707; DOI=10.1039/c1mt00030f;
RA Shafeeq S., Kloosterman T.G., Kuipers O.P.;
RT "Transcriptional response of Streptococcus pneumoniae to Zn2+) limitation
RT and the repressor/activator function of AdcR.";
RL Metallomics 3:609-618(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC, AND SUBUNIT.
RX PubMed=22085181; DOI=10.1021/ja2080532;
RA Guerra A.J., Dann C.E., Giedroc D.P.;
RT "Crystal structure of the zinc-dependent MarR family transcriptional
RT regulator AdcR in the Zn(II)-bound state.";
RL J. Am. Chem. Soc. 133:19614-19617(2011).
CC -!- FUNCTION: Zinc-responsive regulator that acts both as a repressor and
CC as an activator by regulating directly the promoters of its target
CC genes. In the presence of zinc, directly represses the expression of
CC the adcRCBA operon, of genes coding for a group of surface antigen
CC zinc-binding pneumococcal histidine triad proteins (PhtA, PhtB, PhtD
CC and PhtE), and of adcAII. Can also activate expression of adh.
CC {ECO:0000269|PubMed:20804771, ECO:0000269|PubMed:21603707}.
CC -!- ACTIVITY REGULATION: Zinc acts as a coregulator and is required for
CC DNA-binding activity (PubMed:20804771 and PubMed:21603707).
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20804771,
CC ECO:0000269|PubMed:22085181}.
CC -!- MISCELLANEOUS: The second zinc-binding site seems to play no
CC significant role in the regulatory process. Its function is unknown
CC (PubMed:22085181). {ECO:0000305|PubMed:22085181}.
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DR EMBL; CP000410; ABJ54931.1; -; Genomic_DNA.
DR RefSeq; WP_001249319.1; NC_008533.2.
DR PDB; 3TGN; X-ray; 2.00 A; A/B=1-146.
DR PDBsum; 3TGN; -.
DR AlphaFoldDB; Q04I02; -.
DR BMRB; Q04I02; -.
DR SMR; Q04I02; -.
DR STRING; 373153.SPD_2000; -.
DR EnsemblBacteria; ABJ54931; ABJ54931; SPD_2000.
DR GeneID; 60232980; -.
DR GeneID; 66807246; -.
DR KEGG; spd:SPD_2000; -.
DR eggNOG; COG1846; Bacteria.
DR HOGENOM; CLU_142321_1_0_9; -.
DR OMA; INATQAH; -.
DR OrthoDB; 1744037at2; -.
DR BioCyc; SPNE373153:G1G6V-2146-MON; -.
DR Proteomes; UP000001452; 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; IPR001845; HTH_ArsR_DNA-bd_dom.
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; SM00418; HTH_ARSR; 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 3D-structure; Activator; DNA-binding; Metal-binding; Repressor;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..146
FT /note="Transcriptional regulator AdcR"
FT /id="PRO_0000425609"
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:0000269|PubMed:22085181"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22085181"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22085181"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22085181"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22085181"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22085181"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22085181"
FT MUTAGEN 30
FT /note="C->A: Does not affect cellular zinc concentration."
FT /evidence="ECO:0000269|PubMed:20804771"
FT MUTAGEN 42
FT /note="H->A: Strong decrease in zinc binding."
FT /evidence="ECO:0000269|PubMed:20804771"
FT MUTAGEN 108
FT /note="H->Q: Strong decrease in zinc binding. Increases
FT cellular zinc concentration."
FT /evidence="ECO:0000269|PubMed:20804771"
FT MUTAGEN 111
FT /note="H->Q: Does not affect cellular zinc concentration."
FT /evidence="ECO:0000269|PubMed:20804771"
FT MUTAGEN 112
FT /note="H->Q: Strong decrease in zinc binding. Increases
FT cellular zinc concentration."
FT /evidence="ECO:0000269|PubMed:20804771"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:3TGN"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:3TGN"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:3TGN"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:3TGN"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:3TGN"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3TGN"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3TGN"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3TGN"
FT HELIX 102..123
FT /evidence="ECO:0007829|PDB:3TGN"
FT HELIX 128..144
FT /evidence="ECO:0007829|PDB:3TGN"
SQ SEQUENCE 146 AA; 16606 MW; 1368B473BDA01683 CRC64;
MRQLAKDINA FLNEVILQAE NQHEILIGHC TSEVALTNTQ EHILMLLSEE SLTNSELARR
LNVSQAAVTK AIKSLVKEGM LETSKDSKDA RVIFYQLTDL ARPIAEEHHH HHEHTLLTYE
QVATQFTPNE QKVIQRFLTA LVGEIK
