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Protein

Transcriptional repressor SmtB

Gene

smtB

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor of the expression of the smtA gene. Binds two zinc ions per dimer. The complex of DNA and SmtB is dissociated by zinc ions.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi104 – 1041Zinc 1
Metal bindingi106 – 1061Zinc 1
Metal bindingi117 – 1171Zinc 2
Metal bindingi120 – 1201Zinc 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi62 – 8120H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1291-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional repressor SmtB
Gene namesi
Name:smtB
Ordered Locus Names:Synpcc7942_1291
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000002717 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141C → S: Does not abolish zinc binding or metal-induced derepression. 3 Publications
Mutagenesisi61 – 611C → S: Does not abolish zinc binding or metal-induced derepression. 3 Publications
Mutagenesisi105 – 1062HH → RR: Loss of metal-induced derepression. 1 Publication
Mutagenesisi106 – 1061H → Q: Loss of metal-induced derepression. 1 Publication
Mutagenesisi121 – 1211C → S: Does not abolish zinc binding or metal-induced derepression. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Transcriptional repressor SmtBPRO_0000160626Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1291.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 243Combined sources
Helixi30 – 4314Combined sources
Helixi46 – 5510Combined sources
Helixi62 – 698Combined sources
Helixi73 – 8513Combined sources
Beta strandi88 – 947Combined sources
Beta strandi97 – 1048Combined sources
Helixi105 – 11713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R1TX-ray1.70A/B1-122[»]
1R22X-ray2.30A/B1-120[»]
1R23X-ray2.00A/B1-122[»]
1SMTX-ray2.20A/B1-122[»]
ProteinModelPortaliP30340.
SMRiP30340. Positions 18-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30340.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 12295HTH arsR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH arsR-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0640.
HOGENOMiHOG000144506.
OrthoDBiEOG6Z3KS4.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR018334. ArsR_HTH.
IPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01022. HTH_5. 1 hit.
[Graphical view]
PRINTSiPR00778. HTHARSR.
SMARTiSM00418. HTH_ARSR. 1 hit.
[Graphical view]
PROSITEiPS00846. HTH_ARSR_1. 1 hit.
PS50987. HTH_ARSR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30340-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKPVLQDGE TVVCQGTHAA IASELQAIAP EVAQSLAEFF AVLADPNRLR
60 70 80 90 100
LLSLLARSEL CVGDLAQAIG VSESAVSHQL RSLRNLRLVS YRKQGRHVYY
110 120
QLQDHHIVAL YQNALDHLQE CR
Length:122
Mass (Da):13,544
Last modified:April 1, 1993 - v1
Checksum:iA3C98CE13552B93F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64585 Genomic DNA. Translation: CAA45872.1.
CP000100 Genomic DNA. Translation: ABB57321.1.
PIRiS31197.
RefSeqiWP_011242576.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB57321; ABB57321; Synpcc7942_1291.
KEGGisyf:Synpcc7942_1291.
PATRICi23787909. VBISynElo51371_1482.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64585 Genomic DNA. Translation: CAA45872.1.
CP000100 Genomic DNA. Translation: ABB57321.1.
PIRiS31197.
RefSeqiWP_011242576.1. NC_007604.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R1TX-ray1.70A/B1-122[»]
1R22X-ray2.30A/B1-120[»]
1R23X-ray2.00A/B1-122[»]
1SMTX-ray2.20A/B1-122[»]
ProteinModelPortaliP30340.
SMRiP30340. Positions 18-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1291.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB57321; ABB57321; Synpcc7942_1291.
KEGGisyf:Synpcc7942_1291.
PATRICi23787909. VBISynElo51371_1482.

Phylogenomic databases

eggNOGiCOG0640.
HOGENOMiHOG000144506.
OrthoDBiEOG6Z3KS4.

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1291-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP30340.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR018334. ArsR_HTH.
IPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01022. HTH_5. 1 hit.
[Graphical view]
PRINTSiPR00778. HTHARSR.
SMARTiSM00418. HTH_ARSR. 1 hit.
[Graphical view]
PROSITEiPS00846. HTH_ARSR_1. 1 hit.
PS50987. HTH_ARSR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex."
    Morby A.P., Turner J.S., Huckle J.W., Robinson N.J.
    Nucleic Acids Res. 21:921-925(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions."
    Huckle J.W., Morby A.P., Turner J.S., Robinson N.J.
    Mol. Microbiol. 7:177-187(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7942.
  4. "Zn2+-sensing by the cyanobacterial metallothionein repressor SmtB: different motifs mediate metal-induced protein-DNA dissociation."
    Turner J.S., Glands P.D., Samson A.C., Robinson N.J.
    Nucleic Acids Res. 24:3714-3721(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-14; CYS-61; 105-HIS-HIS-106 AND CYS-121.
  5. "The cyanobacterial repressor SmtB is predominantly a dimer and binds two Zn2+ ions per subunit."
    Kar S.R., Adams A.C., Lebowitz J., Taylor K.B., Hall L.M.
    Biochemistry 36:15343-15348(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "Allosteric negative regulation of smt O/P binding of the zinc sensor, SmtB, by metal ions: a coupled equilibrium analysis."
    VanZile M.L., Chen X., Giedroc D.P.
    Biochemistry 41:9776-9786(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-14; CYS-61 AND HIS-106.
  7. "Zinc ions inhibit the protein-DNA complex formation between cyanobacterial transcription factor SmtB and its recognition DNA sequences."
    Morita E.H., Wakamatsu M., Uegaki K., Yumoto N., Kyogoku Y., Hayashi H.
    Plant Cell Physiol. 43:1254-1258(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins."
    Cook W.J., Kar S.R., Taylor K.B., Hall L.M.
    J. Mol. Biol. 275:337-346(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  9. "A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins."
    Eicken C., Pennella M.A., Chen X., Koshlap K.M., VanZile M.L., Sacchettini J.C., Giedroc D.P.
    J. Mol. Biol. 333:683-695(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, MUTAGENESIS OF CYS-14; CYS-61 AND CYS-121.

Entry informationi

Entry nameiSMTB_SYNE7
AccessioniPrimary (citable) accession number: P30340
Secondary accession number(s): Q31NP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 22, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The zinc ions are bound between subunits, so that residues from both subunits contribute to metal binding.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.