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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)DescriptionActionsGraphical viewLength
Metal bindingi104Zinc 11
Metal bindingi106Zinc 11
Metal bindingi117Zinc 21
Metal bindingi120Zinc 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi62 – 81H-T-H motifPROSITE-ProRule annotationAdd BLAST20

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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000002717 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14C → S: Does not abolish zinc binding or metal-induced derepression. 3 Publications1
Mutagenesisi61C → S: Does not abolish zinc binding or metal-induced derepression. 3 Publications1
Mutagenesisi105 – 106HH → RR: Loss of metal-induced derepression. 1 Publication2
Mutagenesisi106H → Q: Loss of metal-induced derepression. 1 Publication1
Mutagenesisi121C → S: Does not abolish zinc binding or metal-induced derepression. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001606261 – 122Transcriptional repressor SmtBAdd BLAST122

Proteomic databases

PRIDEiP30340.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1291.

Structurei

Secondary structure

1122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 24Combined sources3
Helixi30 – 43Combined sources14
Helixi46 – 55Combined sources10
Helixi62 – 69Combined sources8
Helixi73 – 85Combined sources13
Beta strandi88 – 94Combined sources7
Beta strandi97 – 104Combined sources8
Helixi105 – 117Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30340.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 122HTH arsR-typePROSITE-ProRule annotationAdd BLAST95

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107YCR. Bacteria.
COG0640. LUCA.
HOGENOMiHOG000144506.
OrthoDBiPOG091H02HD.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1291.

Proteomic databases

PRIDEiP30340.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4107YCR. Bacteria.
COG0640. LUCA.
HOGENOMiHOG000144506.
OrthoDBiPOG091H02HD.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00846. HTH_ARSR_1. 1 hit.
PS50987. HTH_ARSR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 116 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

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 one 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.