Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30340 (SMTB_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional repressor SmtB
Gene names
Name:smtB
Ordered Locus Names:Synpcc7942_1291
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6 Ref.7

Subunit structure

Homodimer. Ref.5 Ref.9

Miscellaneous

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

Sequence similarities

Contains 1 HTH arsR-type DNA-binding domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122Transcriptional repressor SmtB
PRO_0000160626

Regions

Domain28 – 12295HTH arsR-type
DNA binding62 – 8120H-T-H motif

Sites

Metal binding1041Zinc 1
Metal binding1061Zinc 1
Metal binding1171Zinc 2
Metal binding1201Zinc 2

Experimental info

Mutagenesis141C → S: Does not abolish zinc binding or metal-induced derepression. Ref.4 Ref.6 Ref.9
Mutagenesis611C → S: Does not abolish zinc binding or metal-induced derepression. Ref.4 Ref.6 Ref.9
Mutagenesis105 – 1062HH → RR: Loss of metal-induced derepression. Ref.6
Mutagenesis1061H → Q: Loss of metal-induced derepression. Ref.6
Mutagenesis1211C → S: Does not abolish zinc binding or metal-induced derepression. Ref.4 Ref.9

Secondary structure

................ 122
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30340 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: A3C98CE13552B93F

FASTA12213,544
        10         20         30         40         50         60 
MTKPVLQDGE TVVCQGTHAA IASELQAIAP EVAQSLAEFF AVLADPNRLR LLSLLARSEL 

        70         80         90        100        110        120 
CVGDLAQAIG VSESAVSHQL RSLRNLRLVS YRKQGRHVYY QLQDHHIVAL YQNALDHLQE 


CR 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64585 Genomic DNA. Translation: CAA45872.1.
CP000100 Genomic DNA. Translation: ABB57321.1.
PIRS31197.
RefSeqYP_400308.1. NC_007604.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R1TX-ray1.70A/B1-122[»]
1R22X-ray2.30A/B1-120[»]
1R23X-ray2.00A/B1-122[»]
1SMTX-ray2.20A/B1-122[»]
ProteinModelPortalP30340.
SMRP30340. Positions 18-121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_1291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB57321; ABB57321; Synpcc7942_1291.
GeneID3773580.
KEGGsyf:Synpcc7942_1291.
PATRIC23787909. VBISynElo51371_1482.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0640.
HOGENOMHOG000144506.
OrthoDBEOG6Z3KS4.

Enzyme and pathway databases

BioCycSYNEL:SYNPCC7942_1291-MONOMER.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR018334. ArsR_HTH.
IPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01022. HTH_5. 1 hit.
[Graphical view]
PRINTSPR00778. HTHARSR.
SMARTSM00418. HTH_ARSR. 1 hit.
[Graphical view]
PROSITEPS00846. HTH_ARSR_1. 1 hit.
PS50987. HTH_ARSR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30340.

Entry information

Entry nameSMTB_SYNE7
AccessionPrimary (citable) accession number: P30340
Secondary accession number(s): Q31NP8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: May 14, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references