ZIAR_SYNY3
ID ZIAR_SYNY3 Reviewed; 132 AA.
AC Q55940;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transcriptional repressor SmtB homolog;
GN Name=ziaR; Synonyms=smtB; OrderedLocusNames=sll0792;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP CHARACTERIZATION, AND MUTAGENESIS OF CYS-71; CYS-73 AND HIS-116.
RX PubMed=9724772; DOI=10.1073/pnas.95.18.10728;
RA Thelwell C., Robinson N.J., Turner-Cavet J.S.;
RT "An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc
RT exporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10728-10733(1998).
RN [4]
RP REVIEW.
RX PubMed=12829264; DOI=10.1016/s0168-6445(03)00054-8;
RA Busenlehner L.S., Pennella M.A., Giedroc D.P.;
RT "The SmtB/ArsR family of metalloregulatory transcriptional repressors:
RT Structural insights into prokaryotic metal resistance.";
RL FEMS Microbiol. Rev. 27:131-143(2003).
CC -!- FUNCTION: Transcriptional repressor of the expression of the ziaA gene.
CC Controls zinc homeostasis by triggering ZiaA-mediated efflux of excess
CC zinc into the periplasm.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; BA000022; BAA10706.1; -; Genomic_DNA.
DR PIR; S77014; S77014.
DR AlphaFoldDB; Q55940; -.
DR SMR; Q55940; -.
DR STRING; 1148.1001825; -.
DR PaxDb; Q55940; -.
DR EnsemblBacteria; BAA10706; BAA10706; BAA10706.
DR KEGG; syn:sll0792; -.
DR eggNOG; COG0640; Bacteria.
DR InParanoid; Q55940; -.
DR OMA; HKQGIVK; -.
DR PhylomeDB; Q55940; -.
DR Proteomes; UP000001425; 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; IPR018334; ArsR_HTH.
DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01022; HTH_5; 1.
DR PRINTS; PR00778; HTHARSR.
DR SMART; SM00418; HTH_ARSR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00846; HTH_ARSR_1; 1.
DR PROSITE; PS50987; HTH_ARSR_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..132
FT /note="Transcriptional repressor SmtB homolog"
FT /id="PRO_0000160627"
FT DOMAIN 38..132
FT /note="HTH arsR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT DNA_BIND 72..91
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT MUTAGEN 71
FT /note="C->S: Loss of ability to respond to zinc. Still
FT capable of binding DNA; when associated with S-73."
FT /evidence="ECO:0000269|PubMed:9724772"
FT MUTAGEN 73
FT /note="C->S: Loss of ability to respond to zinc. Still
FT capable of binding DNA; when associated with S-71."
FT /evidence="ECO:0000269|PubMed:9724772"
FT MUTAGEN 116
FT /note="H->R: Loss of ability to respond to zinc. Still
FT capable of binding DNA."
FT /evidence="ECO:0000269|PubMed:9724772"
SQ SEQUENCE 132 AA; 15083 MW; 08A7B19849B186C9 CRC64;
MSKSSLSKSQ SCQNEEMPLC DQPLVHLEQV RQVQPEVMSL DQAQQMAEFF SALADPSRLR
LMSALARQEL CVCDLAAAMK VSESAVSHQL RILRSQRLVK YRRVGRNVYY SLADNHVMNL
YREVADHLQE SD
