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Protein
Submitted name:

C2 toxin (Component I)

Gene
N/A
Organism
Clostridium botulinum
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
C2 toxin (Component I)Imported
OrganismiClostridium botulinumImported
Taxonomic identifieri1491 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J3VX-ray2.11A1-431[»]
2J3XX-ray1.75A1-431[»]
2J3ZX-ray2.30A/B/C/D/E/F1-431[»]
ProteinModelPortaliO69275.
SMRiO69275. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO69275.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini227 – 427201ADPrib_exo_ToxInterPro annotationAdd
BLAST

Family and domain databases

InterProiIPR003540. ADP-ribosyltransferase.
IPR016013. Binary_toxinA_clost-typ.
[Graphical view]
PfamiPF03496. ADPrib_exo_Tox. 1 hit.
[Graphical view]
PRINTSiPR01390. BINARYTOXINA.

Sequencei

Sequence statusi: Complete.

O69275-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIIKEPIDF INKPESEAKK WGKEEEKRWF TKLNNLEEVA VNQLKNKEYK
60 70 80 90 100
TKIDNFSTDI LFSSLTAIEI MKEDENHNLF DVERIREALL KNTLDRDAIG
110 120 130 140 150
YVNFTPKELG INFSIRDVEL NRDISDETLD KVRQQIINQE YTKFSFISLG
160 170 180 190 200
LNDNSINESV PVIVKTRVPT TFDYGVLNDK ETVSLLLNQG FSIIPESAII
210 220 230 240 250
TTIKGKDYIL IEGSLSQELD FYNKGSEAWG AENYGDYISK LSHEQLGALE
260 270 280 290 300
GYLHSDYKAI NSYLRNNRVP NNDELNKKIE LISSALSVKP IPQTLIAYRR
310 320 330 340 350
VDGIPFDLPS DFSFDKKENG EIIADKQKLN EFIDKWTGKE IENLSFSSTS
360 370 380 390 400
LKSTPSSFSK SRFIFRLRLS EGAIGAFIYG FSGFQDEQEI LLNKNSTFKI
410 420 430
FRITPITSII NRVTKMTQVV IDAEGIQNKE I
Length:431
Mass (Da):49,314
Last modified:August 1, 1998 - v1
Checksum:i9CB348771CE038A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224480 Genomic DNA. Translation: CAA11969.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224480 Genomic DNA. Translation: CAA11969.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J3VX-ray2.11A1-431[»]
2J3XX-ray1.75A1-431[»]
2J3ZX-ray2.30A/B/C/D/E/F1-431[»]
ProteinModelPortaliO69275.
SMRiO69275. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO69275.

Family and domain databases

InterProiIPR003540. ADP-ribosyltransferase.
IPR016013. Binary_toxinA_clost-typ.
[Graphical view]
PfamiPF03496. ADPrib_exo_Tox. 1 hit.
[Graphical view]
PRINTSiPR01390. BINARYTOXINA.
ProtoNetiSearch...

Publicationsi

  1. Hofmann F.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 92-13Imported.
  2. "The binary Clostridium botulinum C2 toxin as a protein delivery system: identification of the minimal protein region necessary for interaction of toxin components."
    Barth H., Roebling R., Fritz M., Aktories K.
    J. Biol. Chem. 277:5074-5081(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 92-13Imported.
  3. "Structure and action of the binary C2 toxin from Clostridium botulinum."
    Schleberger C., Hochmann H., Barth H., Aktories K., Schulz G.E.
    J. Mol. Biol. 364:705-715(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

Entry informationi

Entry nameiO69275_CLOBO
AccessioniPrimary (citable) accession number: O69275
Entry historyi
Integrated into UniProtKB/TrEMBL: August 1, 1998
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.