Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Perfringolysin O

Gene

pfo

Organism
Clostridium perfringens (strain 13 / Type A)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A conformation change leads to insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host cell membranes, membrane insertion and pore formation. Can be reversibly inactivated by oxidation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei459 – 4591Binding to cholesterol

GO - Molecular functioni

GO - Biological processi

  • hemolysis in other organism Source: CACAO
  • pathogenesis Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Toxin

Keywords - Biological processi

Cytolysis, Hemolysis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciCPER195102:GJFM-188-MONOMER.

Protein family/group databases

TCDBi1.C.12.1.1. thiol-activated cholesterol-dependent cytolysin (cdc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Perfringolysin O
Alternative name(s):
Theta-toxin
Thiol-activated cytolysin
Gene namesi
Name:pfo
Synonyms:pfoA, pfoR
Ordered Locus Names:CPE0163
OrganismiClostridium perfringens (strain 13 / Type A)
Taxonomic identifieri195102 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000818 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 500472Perfringolysin OPRO_0000034104Add
BLAST

Interactioni

Subunit structurei

Homooligomeric pore complex containing 40-50 subunits; when inserted in the host membrane.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 436Combined sources
Turni49 – 513Combined sources
Beta strandi54 – 563Combined sources
Beta strandi65 – 706Combined sources
Beta strandi72 – 8716Combined sources
Beta strandi90 – 934Combined sources
Turni97 – 993Combined sources
Beta strandi107 – 1093Combined sources
Helixi112 – 1154Combined sources
Beta strandi129 – 1335Combined sources
Turni139 – 1413Combined sources
Beta strandi143 – 1486Combined sources
Helixi151 – 16818Combined sources
Turni169 – 1713Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi178 – 1858Combined sources
Helixi189 – 1968Combined sources
Helixi200 – 2067Combined sources
Helixi211 – 2155Combined sources
Beta strandi218 – 23518Combined sources
Helixi241 – 2444Combined sources
Helixi251 – 2566Combined sources
Beta strandi260 – 2634Combined sources
Beta strandi265 – 28420Combined sources
Helixi290 – 29910Combined sources
Helixi302 – 3054Combined sources
Helixi307 – 3148Combined sources
Beta strandi316 – 3249Combined sources
Turni328 – 3314Combined sources
Beta strandi333 – 3364Combined sources
Helixi338 – 34710Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi359 – 3668Combined sources
Turni367 – 3693Combined sources
Beta strandi377 – 39014Combined sources
Beta strandi392 – 3987Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi404 – 41512Combined sources
Beta strandi421 – 4277Combined sources
Turni429 – 4324Combined sources
Beta strandi437 – 4459Combined sources
Beta strandi449 – 45810Combined sources
Beta strandi461 – 4633Combined sources
Helixi464 – 4663Combined sources
Beta strandi469 – 4757Combined sources
Beta strandi480 – 4889Combined sources
Beta strandi490 – 49910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3IX-ray2.90A/B/C/D30-500[»]
1M3JX-ray3.00A/B30-500[»]
1PFOX-ray2.20A1-500[»]
2BK1electron microscopy29.00A53-500[»]
2BK2electron microscopy28.00A36-500[»]
DisProtiDP00280.
ProteinModelPortaliP0C2E9.
SMRiP0C2E9. Positions 30-500.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2E9.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiol-activated cytolysin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

HOGENOMiHOG000056095.
KOiK11031.
OMAiLTYNNQE.
OrthoDBiPOG091H0PSV.

Family and domain databases

Gene3Di3.90.840.10. 4 hits.
InterProiIPR001869. Thiol_cytolysin.
[Graphical view]
PfamiPF01289. Thiol_cytolysin. 1 hit.
[Graphical view]
PRINTSiPR01400. TACYTOLYSIN.
SUPFAMiSSF56978. SSF56978. 1 hit.
PROSITEiPS00481. THIOL_CYTOLYSINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C2E9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRFKKTKLI ASIAMALCLF SQPVISFSKD ITDKNQSIDS GISSLSYNRN
60 70 80 90 100
EVLASNGDKI ESFVPKEGKK TGNKFIVVER QKRSLTTSPV DISIIDSVND
110 120 130 140 150
RTYPGALQLA DKAFVENRPT ILMVKRKPIN INIDLPGLKG ENSIKVDDPT
160 170 180 190 200
YGKVSGAIDE LVSKWNEKYS STHTLPARTQ YSESMVYSKS QISSALNVNA
210 220 230 240 250
KVLENSLGVD FNAVANNEKK VMILAYKQIF YTVSADLPKN PSDLFDDSVT
260 270 280 290 300
FNDLKQKGVS NEAPPLMVSN VAYGRTIYVK LETTSSSKDV QAAFKALIKN
310 320 330 340 350
TDIKNSQQYK DIYENSSFTA VVLGGDAQEH NKVVTKDFDE IRKVIKDNAT
360 370 380 390 400
FSTKNPAYPI SYTSVFLKDN SVAAVHNKTD YIETTSTEYS KGKINLDHSG
410 420 430 440 450
AYVAQFEVAW DEVSYDKEGN EVLTHKTWDG NYQDKTAHYS TVIPLEANAR
460 470 480 490 500
NIRIKARECT GLAWEWWRDV ISEYDVPLTN NINVSIWGTT LYPGSSITYN
Length:500
Mass (Da):55,830
Last modified:January 23, 2007 - v1
Checksum:iE5584B7347413EF2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301D → K AA sequence (PubMed:2878682).Curated
Sequence conflicti34 – 341K → I AA sequence (PubMed:2878682).Curated
Sequence conflicti71 – 711T → A in AAA23271 (PubMed:1987025).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81080 Genomic DNA. Translation: AAA23271.1.
BA000016 Genomic DNA. Translation: BAB79869.1.
PIRiB43577.
RefSeqiWP_003467630.1. NC_003366.1.

Genome annotation databases

EnsemblBacteriaiBAB79869; BAB79869; BAB79869.
GeneIDi988404.
KEGGicpe:CPE0163.
PATRICi19494208. VBICloPer59675_0221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81080 Genomic DNA. Translation: AAA23271.1.
BA000016 Genomic DNA. Translation: BAB79869.1.
PIRiB43577.
RefSeqiWP_003467630.1. NC_003366.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3IX-ray2.90A/B/C/D30-500[»]
1M3JX-ray3.00A/B30-500[»]
1PFOX-ray2.20A1-500[»]
2BK1electron microscopy29.00A53-500[»]
2BK2electron microscopy28.00A36-500[»]
DisProtiDP00280.
ProteinModelPortaliP0C2E9.
SMRiP0C2E9. Positions 30-500.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.C.12.1.1. thiol-activated cholesterol-dependent cytolysin (cdc) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB79869; BAB79869; BAB79869.
GeneIDi988404.
KEGGicpe:CPE0163.
PATRICi19494208. VBICloPer59675_0221.

Phylogenomic databases

HOGENOMiHOG000056095.
KOiK11031.
OMAiLTYNNQE.
OrthoDBiPOG091H0PSV.

Enzyme and pathway databases

BioCyciCPER195102:GJFM-188-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0C2E9.

Family and domain databases

Gene3Di3.90.840.10. 4 hits.
InterProiIPR001869. Thiol_cytolysin.
[Graphical view]
PfamiPF01289. Thiol_cytolysin. 1 hit.
[Graphical view]
PRINTSiPR01400. TACYTOLYSIN.
SUPFAMiSSF56978. SSF56978. 1 hit.
PROSITEiPS00481. THIOL_CYTOLYSINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTACY_CLOPE
AccessioniPrimary (citable) accession number: P0C2E9
Secondary accession number(s): P19995
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 68 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

3D-structure, Complete proteome, Direct protein sequencing, 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.