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P30340

- SMTB_SYNE7

UniProt

P30340 - SMTB_SYNE7

Protein

Transcriptional repressor SmtB

Gene

smtB

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. sequence-specific DNA binding transcription factor activity Source: InterPro

    GO - Biological processi

    1. transcription, DNA-templated Source: UniProtKB-KW

    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: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: InterPro

    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.
    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 – 243
    Helixi30 – 4314
    Helixi46 – 5510
    Helixi62 – 698
    Helixi73 – 8513
    Beta strandi88 – 947
    Beta strandi97 – 1048
    Helixi105 – 11713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MTKPVLQDGE TVVCQGTHAA IASELQAIAP EVAQSLAEFF AVLADPNRLR    50
    LLSLLARSEL CVGDLAQAIG VSESAVSHQL RSLRNLRLVS YRKQGRHVYY 100
    QLQDHHIVAL YQNALDHLQE CR 122
    Length:122
    Mass (Da):13,544
    Last modified:April 1, 1993 - v1
    Checksum:iA3C98CE13552B93F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64585 Genomic DNA. Translation: CAA45872.1.
    CP000100 Genomic DNA. Translation: ABB57321.1.
    PIRiS31197.
    RefSeqiYP_400308.1. NC_007604.1.

    Genome annotation databases

    EnsemblBacteriaiABB57321; ABB57321; Synpcc7942_1291.
    GeneIDi3773580.
    KEGGisyf:Synpcc7942_1291.
    PATRICi23787909. VBISynElo51371_1482.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64585 Genomic DNA. Translation: CAA45872.1 .
    CP000100 Genomic DNA. Translation: ABB57321.1 .
    PIRi S31197.
    RefSeqi YP_400308.1. NC_007604.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R1T X-ray 1.70 A/B 1-122 [» ]
    1R22 X-ray 2.30 A/B 1-120 [» ]
    1R23 X-ray 2.00 A/B 1-122 [» ]
    1SMT X-ray 2.20 A/B 1-122 [» ]
    ProteinModelPortali P30340.
    SMRi P30340. Positions 18-121.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 1140.Synpcc7942_1291.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB57321 ; ABB57321 ; Synpcc7942_1291 .
    GeneIDi 3773580.
    KEGGi syf:Synpcc7942_1291.
    PATRICi 23787909. VBISynElo51371_1482.

    Phylogenomic databases

    eggNOGi COG0640.
    HOGENOMi HOG000144506.
    OrthoDBi EOG6Z3KS4.

    Enzyme and pathway databases

    BioCyci SYNEL:SYNPCC7942_1291-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P30340.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR018334. ArsR_HTH.
    IPR001845. HTH_ArsR_DNA-bd_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01022. HTH_5. 1 hit.
    [Graphical view ]
    PRINTSi PR00778. HTHARSR.
    SMARTi SM00418. HTH_ARSR. 1 hit.
    [Graphical view ]
    PROSITEi PS00846. HTH_ARSR_1. 1 hit.
    PS50987. HTH_ARSR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 101 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