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Protein

Streptolysin O

Gene

slo

Organism
Streptococcus pyogenes serotype M1
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Can be reversibly inactivated by oxidation (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei530 – 5301Binding to cholesterolBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Toxin

Keywords - Biological processi

Cytolysis, Hemolysis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciSPYO160490:GJ81-168-MONOMER.
SPYO293653:GHFC-191-MONOMER.

Protein family/group databases

TCDBi1.C.12.1.4. thiol-activated cholesterol-dependent cytolysin (cdc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Streptolysin O
Alternative name(s):
Thiol-activated cytolysin
Gene namesi
Name:slo
Ordered Locus Names:SPy_0167, M5005_Spy0141
OrganismiStreptococcus pyogenes serotype M1
Taxonomic identifieri301447 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000750 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 – 3333Sequence analysisAdd
BLAST
Chaini34 – 571538Streptolysin OPRO_0000041941Add
BLAST

Proteomic databases

PaxDbiP0C0I3.

Interactioni

Subunit structurei

Homooligomeric pore complex; when inserted in the host membrane.By similarity

Protein-protein interaction databases

STRINGi160490.SPy_0167.

Structurei

3D structure databases

ProteinModelPortaliP0C0I3.
SMRiP0C0I3. Positions 107-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiol-activated cytolysin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105E5P. Bacteria.
ENOG410XQPX. LUCA.
HOGENOMiHOG000056095.
KOiK11031.
OMAiLTYNNQE.
OrthoDBiEOG6S7XT6.

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.

P0C0I3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKKTFKKY SRVAGLLTAA LIIGNLVTAN AESNKQNTAS TETTTTNEQP
60 70 80 90 100
KPESSELTTE KAGQKTDDML NSNDMIKLAP KEMPLESAEK EEKKSEDKKK
110 120 130 140 150
SEEDHTEEIN DKIYSLNYNE LEVLAKNGET IENFVPKEGV KKADKFIVIE
160 170 180 190 200
RKKKNINTTP VDISIIDSVT DRTYPAALQL ANKGFTENKP DAVVTKRNPQ
210 220 230 240 250
KIHIDLPGMG DKATVEVNDP TYANVSTAID NLVNQWHDNY SGGNTLPART
260 270 280 290 300
QYTESMVYSK SQIEAALNVN SKILDGTLGI DFKSISKGEK KVMIAAYKQI
310 320 330 340 350
FYTVSANLPN NPADVFDKSV TFKELQRKGV SNEAPPLFVS NVAYGRTVFV
360 370 380 390 400
KLETSSKSND VEAAFSAALK GTDVKTNGKY SDILENSSFT AVVLGGDAAE
410 420 430 440 450
HNKVVTKDFD VIRNVIKDNA TFSRKNPAYP ISYTSVFLKN NKIAGVNNRT
460 470 480 490 500
EYVETTSTEY TSGKINLSHQ GAYVAQYEIL WDEINYDDKG KEVITKRRWD
510 520 530 540 550
NNWYSKTSPF STVIPLGANS RNIRIMAREC TGLAWEWWRK VIDERDVKLS
560 570
KEINVNISGS TLSPYGSITY K
Length:571
Mass (Da):63,638
Last modified:September 13, 2005 - v1
Checksum:iD05AA9979DCBCAB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661T → M in AAZ50760 (PubMed:16088826).Curated
Sequence conflicti450 – 4501T → S in AAZ50760 (PubMed:16088826).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK33267.1.
CP000017 Genomic DNA. Translation: AAZ50760.1.
RefSeqiNP_268546.1. NC_002737.2.

Genome annotation databases

EnsemblBacteriaiAAK33267; AAK33267; SPy_0167.
AAZ50760; AAZ50760; M5005_Spy0141.
GeneIDi900490.
KEGGispy:SPy_0167.
spz:M5005_Spy0141.
PATRICi19714139. VBIStrPyo79812_0145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK33267.1.
CP000017 Genomic DNA. Translation: AAZ50760.1.
RefSeqiNP_268546.1. NC_002737.2.

3D structure databases

ProteinModelPortaliP0C0I3.
SMRiP0C0I3. Positions 107-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160490.SPy_0167.

Protein family/group databases

TCDBi1.C.12.1.4. thiol-activated cholesterol-dependent cytolysin (cdc) family.

Proteomic databases

PaxDbiP0C0I3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK33267; AAK33267; SPy_0167.
AAZ50760; AAZ50760; M5005_Spy0141.
GeneIDi900490.
KEGGispy:SPy_0167.
spz:M5005_Spy0141.
PATRICi19714139. VBIStrPyo79812_0145.

Phylogenomic databases

eggNOGiENOG4105E5P. Bacteria.
ENOG410XQPX. LUCA.
HOGENOMiHOG000056095.
KOiK11031.
OMAiLTYNNQE.
OrthoDBiEOG6S7XT6.

Enzyme and pathway databases

BioCyciSPYO160490:GJ81-168-MONOMER.
SPYO293653:GHFC-191-MONOMER.

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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700294 / SF370 / Serotype M1.
  2. "Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events."
    Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M.
    J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

Entry informationi

Entry nameiTACY_STRP1
AccessioniPrimary (citable) accession number: P0C0I3
Secondary accession number(s): P0A4K9, P21131, Q491F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: April 13, 2016
This is version 73 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

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.