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Protein
Submitted name:

Regulatory protein

Gene

esp1396IC

Organism
Enterobacter sp. RFL1396
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
Complete GO annotation...

Protein family/group databases

REBASEi17355. C.Esp1396I.

Names & Taxonomyi

Protein namesi
Submitted name:
Regulatory proteinImported
Gene namesi
Name:esp1396ICImported
Encoded oniPlasmid pEsp1396Imported
OrganismiEnterobacter sp. RFL1396Imported
Taxonomic identifieri211595 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CLCX-ray2.80A/B/C/D1-79[»]
3FYAX-ray3.00A/B1-79[»]
3G5GX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N1-79[»]
3S8QX-ray2.10A/B1-79[»]
3UFDX-ray2.80A/B/E/F1-79[»]
4F8DX-ray1.50A/B1-79[»]
4FBIX-ray1.50A/B/C/D1-79[»]
4FN3X-ray1.79A/B1-79[»]
4I6RX-ray1.38A/B1-79[»]
4I6TX-ray2.00A/B1-79[»]
4I6UX-ray1.97A/B/C/D/E/F1-79[»]
4I8TX-ray3.00A/B1-79[»]
4IA8X-ray1.85A/B1-79[»]
4IVZX-ray3.10A/B/E/F1-79[»]
4IWRX-ray2.40A/B/E/F1-79[»]
ProteinModelPortaliQ8GGH0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GGH0.

Family & Domainsi

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
PfamiPF01381. HTH_3. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8GGH0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESFLLSKVS FVIKKIRLEK GMTQEDLAYK SNLDRTYISG IERNSRNLTI
60 70
KSLELIMKGL EVSDVVFFEM LIKEILKHD
Length:79
Mass (Da):9,225
Last modified:March 1, 2003 - v1
Checksum:iB4DDF13A4F9E6998
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF527822 Genomic DNA. Translation: AAO16093.1.
RefSeqiNP_862207.1. NC_004936.1.
WP_011116951.1. NC_004936.1.

Genome annotation databases

GeneIDi1482839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF527822 Genomic DNA. Translation: AAO16093.1.
RefSeqiNP_862207.1. NC_004936.1.
WP_011116951.1. NC_004936.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CLCX-ray2.80A/B/C/D1-79[»]
3FYAX-ray3.00A/B1-79[»]
3G5GX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N1-79[»]
3S8QX-ray2.10A/B1-79[»]
3UFDX-ray2.80A/B/E/F1-79[»]
4F8DX-ray1.50A/B1-79[»]
4FBIX-ray1.50A/B/C/D1-79[»]
4FN3X-ray1.79A/B1-79[»]
4I6RX-ray1.38A/B1-79[»]
4I6TX-ray2.00A/B1-79[»]
4I6UX-ray1.97A/B/C/D/E/F1-79[»]
4I8TX-ray3.00A/B1-79[»]
4IA8X-ray1.85A/B1-79[»]
4IVZX-ray3.10A/B/E/F1-79[»]
4IWRX-ray2.40A/B/E/F1-79[»]
ProteinModelPortaliQ8GGH0.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi17355. C.Esp1396I.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1482839.

Miscellaneous databases

EvolutionaryTraceiQ8GGH0.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
PfamiPF01381. HTH_3. 1 hit.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Esp1396I restriction-modification system: structural organization and mode of regulation."
    Cesnaviciene E., Mitkaite G., Stankevicius K., Janulaitis A., Lubys A.
    Nucleic Acids Res. 31:743-749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: RFL1396Imported.
    Plasmid: pEsp1396
  2. "Structural analysis of the genetic switch that regulates the expression of restriction-modification genes."
    McGeehan J.E., Streeter S.D., Thresh S.J., Ball N., Ravelli R.B., Kneale G.G.
    Nucleic Acids Res. 36:4778-4787(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
  3. "Structure of the restriction-modification controller protein C.Esp1396I."
    Ball N., Streeter S.D., Kneale G.G., McGeehan J.E.
    Acta Crystallogr. D 65:900-905(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
  4. "Recognition of dual symmetry by the controller protein C.Esp1396I based on the structure of the transcriptional activation complex."
    McGeehan J.E., Ball N.J., Streeter S.D., Thresh S.J., Kneale G.G.
    Nucleic Acids Res. 40:4158-4167(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
  5. "The structural basis of differential DNA sequence recognition by restriction-modification controller proteins."
    Ball N.J., McGeehan J.E., Streeter S.D., Thresh S.J., Kneale G.G.
    Nucleic Acids Res. 40:10532-10542(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
  6. "Structural analysis of DNA-protein complexes regulating the restriction-modification system Esp1396I."
    Martin R.N., McGeehan J.E., Ball N.J., Streeter S.D., Thresh S.J., Kneale G.G.
    Acta Crystallogr. F 69:962-966(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
  7. "Structural and mutagenic analysis of the RM controller protein C.Esp1396I."
    Martin R.N., McGeehan J.E., Kneale G.
    PLoS ONE 9:e98365-e98365(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS).

Entry informationi

Entry nameiQ8GGH0_9ENTR
AccessioniPrimary (citable) accession number: Q8GGH0
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: January 7, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, PlasmidImported

External Data

Dasty 3

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 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.