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Protein

Transcriptional repressor SmtB homolog

Gene

ziaR

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor of the expression of the ziaA gene. Controls zinc homeostasis by triggering ZiaA-mediated efflux of excess zinc into the periplasm.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi20ZincPROSITE-ProRule annotation1
Metal bindingi26ZincPROSITE-ProRule annotation1
Metal bindingi71ZincPROSITE-ProRule annotation1
Metal bindingi73ZincPROSITE-ProRule annotation1
Metal bindingi114ZincPROSITE-ProRule annotation1
Metal bindingi116ZincPROSITE-ProRule annotation1
Metal bindingi127ZincPROSITE-ProRule annotation1
Metal bindingi130ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi72 – 91H-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

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional repressor SmtB homolog
Gene namesi
Name:ziaR
Synonyms:smtB
Ordered Locus Names:sll0792
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi71C → S: Loss of ability to respond to zinc. Still capable of binding DNA; when associated with S-73. 1 Publication1
Mutagenesisi73C → S: Loss of ability to respond to zinc. Still capable of binding DNA; when associated with S-71. 1 Publication1
Mutagenesisi116H → R: Loss of ability to respond to zinc. Still capable of binding DNA. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001606271 – 132Transcriptional repressor SmtB homologAdd BLAST132

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ55940.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 132HTH arsR-typePROSITE-ProRule annotationAdd BLAST95

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000144506.
InParanoidiQ55940.
OMAiLMANREG.
PhylomeDBiQ55940.

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.

Q55940-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSSLSKSQ SCQNEEMPLC DQPLVHLEQV RQVQPEVMSL DQAQQMAEFF
60 70 80 90 100
SALADPSRLR LMSALARQEL CVCDLAAAMK VSESAVSHQL RILRSQRLVK
110 120 130
YRRVGRNVYY SLADNHVMNL YREVADHLQE SD
Length:132
Mass (Da):15,083
Last modified:November 1, 1996 - v1
Checksum:i08A7B19849B186C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10706.1.
PIRiS77014.

Genome annotation databases

EnsemblBacteriaiBAA10706; BAA10706; BAA10706.
KEGGisyn:sll0792.
PATRICi23843014. VBISynSp132158_3045.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10706.1.
PIRiS77014.

3D structure databases

ProteinModelPortaliQ55940.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10706; BAA10706; BAA10706.
KEGGisyn:sll0792.
PATRICi23843014. VBISynSp132158_3045.

Phylogenomic databases

HOGENOMiHOG000144506.
InParanoidiQ55940.
OMAiLMANREG.
PhylomeDBiQ55940.

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 nameiZIAR_SYNY3
AccessioniPrimary (citable) accession number: Q55940
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.