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Protein

Transcriptional repressor SmtB

Gene

smtB

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-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

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

Phylogenomic databases

eggNOGiENOG4107YCR Bacteria
COG0640 LUCA
HOGENOMiHOG000144506
KOiK21903
OrthoDBiPOG091H02HD

Family and domain databases

CDDicd00090 HTH_ARSR, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR011991 ArsR-like_HTH
IPR018334 ArsR_HTH
IPR001845 HTH_ArsR_DNA-bd_dom
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF01022 HTH_5, 1 hit
PRINTSiPR00778 HTHARSR
SMARTiView protein in SMART
SM00418 HTH_ARSR, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS00846 HTH_ARSR_1, 1 hit
PS50987 HTH_ARSR_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiSMTB_SYNE7
AccessioniPrimary (citable) accession number: P30340
Secondary accession number(s): Q31NP8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: January 31, 2018
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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