SMTB_SYNE7
ID SMTB_SYNE7 Reviewed; 122 AA.
AC P30340; Q31NP8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Transcriptional repressor SmtB;
GN Name=smtB; OrderedLocusNames=Synpcc7942_1291;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8451191; DOI=10.1093/nar/21.4.921;
RA Morby A.P., Turner J.S., Huckle J.W., Robinson N.J.;
RT "SmtB is a metal-dependent repressor of the cyanobacterial metallothionein
RT gene smtA: identification of a Zn inhibited DNA-protein complex.";
RL Nucleic Acids Res. 21:921-925(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8446025; DOI=10.1111/j.1365-2958.1993.tb01109.x;
RA Huckle J.W., Morby A.P., Turner J.S., Robinson N.J.;
RT "Isolation of a prokaryotic metallothionein locus and analysis of
RT transcriptional control by trace metal ions.";
RL Mol. Microbiol. 7:177-187(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND MUTAGENESIS OF CYS-14; CYS-61; 105-HIS-HIS-106 AND CYS-121.
RX PubMed=8871549; DOI=10.1093/nar/24.19.3714;
RA Turner J.S., Glands P.D., Samson A.C., Robinson N.J.;
RT "Zn2+-sensing by the cyanobacterial metallothionein repressor SmtB:
RT different motifs mediate metal-induced protein-DNA dissociation.";
RL Nucleic Acids Res. 24:3714-3721(1996).
RN [5]
RP SUBUNIT.
RX PubMed=9398263; DOI=10.1021/bi971690v;
RA Kar S.R., Adams A.C., Lebowitz J., Taylor K.B., Hall L.M.;
RT "The cyanobacterial repressor SmtB is predominantly a dimer and binds two
RT Zn2+ ions per subunit.";
RL Biochemistry 36:15343-15348(1997).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-14; CYS-61 AND HIS-106.
RX PubMed=12146943; DOI=10.1021/bi020178t;
RA VanZile M.L., Chen X., Giedroc D.P.;
RT "Allosteric negative regulation of smt O/P binding of the zinc sensor,
RT SmtB, by metal ions: a coupled equilibrium analysis.";
RL Biochemistry 41:9776-9786(2002).
RN [7]
RP FUNCTION.
RX PubMed=12407207; DOI=10.1093/pcp/pcf140;
RA Morita E.H., Wakamatsu M., Uegaki K., Yumoto N., Kyogoku Y., Hayashi H.;
RT "Zinc ions inhibit the protein-DNA complex formation between cyanobacterial
RT transcription factor SmtB and its recognition DNA sequences.";
RL Plant Cell Physiol. 43:1254-1258(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9466913; DOI=10.1006/jmbi.1997.1443;
RA Cook W.J., Kar S.R., Taylor K.B., Hall L.M.;
RT "Crystal structure of the cyanobacterial metallothionein repressor SmtB: a
RT model for metalloregulatory proteins.";
RL J. Mol. Biol. 275:337-346(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT,
RP AND MUTAGENESIS OF CYS-14; CYS-61 AND CYS-121.
RX PubMed=14568530; DOI=10.1016/j.jmb.2003.09.007;
RA Eicken C., Pennella M.A., Chen X., Koshlap K.M., VanZile M.L.,
RA Sacchettini J.C., Giedroc D.P.;
RT "A metal-ligand-mediated intersubunit allosteric switch in related
RT SmtB/ArsR zinc sensor proteins.";
RL J. Mol. Biol. 333:683-695(2003).
CC -!- FUNCTION: Transcriptional repressor of the expression of the smtA gene.
CC Binds two zinc ions per dimer. The complex of DNA and SmtB is
CC dissociated by zinc ions. {ECO:0000269|PubMed:12146943,
CC ECO:0000269|PubMed:12407207, ECO:0000269|PubMed:8871549}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14568530,
CC ECO:0000269|PubMed:9398263}.
CC -!- MISCELLANEOUS: The zinc ions are bound between subunits, so that
CC residues from both subunits contribute to metal binding.
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DR EMBL; X64585; CAA45872.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57321.1; -; Genomic_DNA.
DR PIR; S31197; S31197.
DR RefSeq; WP_011242576.1; NC_007604.1.
DR PDB; 1R1T; X-ray; 1.70 A; A/B=1-122.
DR PDB; 1R22; X-ray; 2.30 A; A/B=1-120.
DR PDB; 1R23; X-ray; 2.00 A; A/B=1-122.
DR PDB; 1SMT; X-ray; 2.20 A; A/B=1-122.
DR PDBsum; 1R1T; -.
DR PDBsum; 1R22; -.
DR PDBsum; 1R23; -.
DR PDBsum; 1SMT; -.
DR AlphaFoldDB; P30340; -.
DR BMRB; P30340; -.
DR SMR; P30340; -.
DR STRING; 1140.Synpcc7942_1291; -.
DR PRIDE; P30340; -.
DR EnsemblBacteria; ABB57321; ABB57321; Synpcc7942_1291.
DR KEGG; syf:Synpcc7942_1291; -.
DR eggNOG; COG0640; Bacteria.
DR HOGENOM; CLU_097806_7_3_3; -.
DR OMA; YHVEHLR; -.
DR OrthoDB; 1772343at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1291-MON; -.
DR EvolutionaryTrace; P30340; -.
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 3D-structure; DNA-binding; Metal-binding; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..122
FT /note="Transcriptional repressor SmtB"
FT /id="PRO_0000160626"
FT DOMAIN 28..122
FT /note="HTH arsR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT DNA_BIND 62..81
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT MUTAGEN 14
FT /note="C->S: Does not abolish zinc binding or metal-induced
FT derepression."
FT /evidence="ECO:0000269|PubMed:12146943,
FT ECO:0000269|PubMed:14568530, ECO:0000269|PubMed:8871549"
FT MUTAGEN 61
FT /note="C->S: Does not abolish zinc binding or metal-induced
FT derepression."
FT /evidence="ECO:0000269|PubMed:12146943,
FT ECO:0000269|PubMed:14568530, ECO:0000269|PubMed:8871549"
FT MUTAGEN 105..106
FT /note="HH->RR: Loss of metal-induced derepression."
FT /evidence="ECO:0000269|PubMed:8871549"
FT MUTAGEN 106
FT /note="H->Q: Loss of metal-induced derepression."
FT /evidence="ECO:0000269|PubMed:12146943"
FT MUTAGEN 121
FT /note="C->S: Does not abolish zinc binding or metal-induced
FT derepression."
FT /evidence="ECO:0000269|PubMed:14568530,
FT ECO:0000269|PubMed:8871549"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1R23"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:1R1T"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:1R1T"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:1R1T"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:1R1T"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1R1T"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1R1T"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:1R1T"
SQ SEQUENCE 122 AA; 13544 MW; A3C98CE13552B93F CRC64;
MTKPVLQDGE TVVCQGTHAA IASELQAIAP EVAQSLAEFF AVLADPNRLR LLSLLARSEL
CVGDLAQAIG VSESAVSHQL RSLRNLRLVS YRKQGRHVYY QLQDHHIVAL YQNALDHLQE
CR
