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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)DescriptionActionsGraphical viewLength
Sitei459Binding to cholesterol1

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

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000003410429 – 500Perfringolysin OAdd BLAST472

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1500
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 43Combined sources6
Turni49 – 51Combined sources3
Beta strandi54 – 56Combined sources3
Beta strandi65 – 70Combined sources6
Beta strandi72 – 87Combined sources16
Beta strandi90 – 93Combined sources4
Turni97 – 99Combined sources3
Beta strandi107 – 109Combined sources3
Helixi112 – 115Combined sources4
Beta strandi129 – 133Combined sources5
Turni139 – 141Combined sources3
Beta strandi143 – 148Combined sources6
Helixi151 – 168Combined sources18
Turni169 – 171Combined sources3
Beta strandi174 – 176Combined sources3
Beta strandi178 – 185Combined sources8
Helixi189 – 196Combined sources8
Helixi200 – 206Combined sources7
Helixi211 – 215Combined sources5
Beta strandi218 – 235Combined sources18
Helixi241 – 244Combined sources4
Helixi251 – 256Combined sources6
Beta strandi260 – 263Combined sources4
Beta strandi265 – 284Combined sources20
Helixi290 – 299Combined sources10
Helixi302 – 305Combined sources4
Helixi307 – 314Combined sources8
Beta strandi316 – 324Combined sources9
Turni328 – 331Combined sources4
Beta strandi333 – 336Combined sources4
Helixi338 – 347Combined sources10
Beta strandi350 – 352Combined sources3
Beta strandi359 – 366Combined sources8
Turni367 – 369Combined sources3
Beta strandi377 – 390Combined sources14
Beta strandi392 – 398Combined sources7
Beta strandi400 – 402Combined sources3
Beta strandi404 – 415Combined sources12
Beta strandi421 – 427Combined sources7
Turni429 – 432Combined sources4
Beta strandi437 – 445Combined sources9
Beta strandi449 – 458Combined sources10
Beta strandi461 – 463Combined sources3
Helixi464 – 466Combined sources3
Beta strandi469 – 475Combined sources7
Beta strandi480 – 488Combined sources9
Beta strandi490 – 499Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti30D → K AA sequence (PubMed:2878682).Curated1
Sequence conflicti34K → I AA sequence (PubMed:2878682).Curated1
Sequence conflicti71T → A in AAA23271 (PubMed:1987025).Curated1

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.
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
PDB 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.
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.
KEGGicpe:CPE0163.
PATRICi19494208. VBICloPer59675_0221.

Phylogenomic databases

HOGENOMiHOG000056095.
KOiK11031.
OMAiLTYNNQE.
OrthoDBiPOG091H0PSV.

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: November 30, 2016
This is version 71 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.