TACY_STRR6
ID TACY_STRR6 Reviewed; 471 AA.
AC Q7ZAK5;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pneumolysin;
DE Short=PLY;
DE AltName: Full=Thiol-activated cytolysin;
GN Name=ply; OrderedLocusNames=spr1739;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-255 / R6;
RX DOI=10.1111/j.1574-6968.1977.tb00951.x;
RA Johnson M.K.;
RT "Cellular location of pneumolysin.";
RL (er) FEMS Microbiol. Lett. 2:243-245(1977).
CC -!- FUNCTION: A cholesterol-dependent toxin that causes cytolysis by
CC forming pores in cholesterol containing host membranes. After binding
CC to target membranes, the protein undergoes a major conformation change,
CC leading to its insertion in the host membrane and formation of an
CC oligomeric pore complex. Cholesterol is required for binding to host
CC membranes, membrane insertion and pore formation; cholesterol binding
CC is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly
CC inactivated by oxidation. {ECO:0000250|UniProtKB:P13128}.
CC -!- SUBUNIT: Homooligomeric pore complex of 35 to 50 subunits; when
CC inserted in the host membrane. {ECO:0000250|UniProtKB:Q04IN8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.2}. Secreted
CC {ECO:0000250|UniProtKB:P0C2J9}. Host cell membrane
CC {ECO:0000250|UniProtKB:P13128}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q04IN8}. Note=Probably secreted as soluble
CC protein by the accessory Sec system (By similarity). It then inserts
CC into the host cell membrane and forms pores formed by transmembrane
CC beta-strands (By similarity). {ECO:0000250|UniProtKB:P0C2J9,
CC ECO:0000250|UniProtKB:Q04IN8}.
CC -!- SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.
CC {ECO:0000305}.
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DR EMBL; AE007317; AAL00542.1; -; Genomic_DNA.
DR PIR; F95224; F95224.
DR RefSeq; NP_359331.1; NC_003098.1.
DR RefSeq; WP_001284359.1; NC_003098.1.
DR AlphaFoldDB; Q7ZAK5; -.
DR SMR; Q7ZAK5; -.
DR STRING; 171101.spr1739; -.
DR PRIDE; Q7ZAK5; -.
DR ABCD; Q7ZAK5; 5 sequenced antibodies.
DR EnsemblBacteria; AAL00542; AAL00542; spr1739.
DR GeneID; 60232858; -.
DR GeneID; 66806991; -.
DR KEGG; spr:spr1739; -.
DR PATRIC; fig|171101.6.peg.1883; -.
DR eggNOG; ENOG502Z7ST; Bacteria.
DR HOGENOM; CLU_026912_1_0_9; -.
DR OMA; NDRTYPG; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015485; F:cholesterol binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1430; -; 1.
DR Gene3D; 3.90.840.10; -; 1.
DR InterPro; IPR035390; Thiol_cytolys_C.
DR InterPro; IPR038700; Thiol_cytolys_C_sf.
DR InterPro; IPR001869; Thiol_cytolysin.
DR InterPro; IPR036363; Thiol_cytolysin_ab_sf.
DR InterPro; IPR036359; Thiol_cytolysin_sf.
DR Pfam; PF17440; Thiol_cytolys_C; 1.
DR Pfam; PF01289; Thiol_cytolysin; 1.
DR PRINTS; PR01400; TACYTOLYSIN.
DR SUPFAM; SSF56978; SSF56978; 1.
DR PROSITE; PS00481; THIOL_CYTOLYSINS; 1.
PE 3: Inferred from homology;
KW Cytolysis; Cytoplasm; Hemolysis; Host cell membrane; Host membrane;
KW Lipid-binding; Membrane; Reference proteome; Secreted; Toxin;
KW Transmembrane; Transmembrane beta strand; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..471
FT /note="Pneumolysin"
FT /id="PRO_0000279547"
FT TRANSMEM 158..171
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 178..187
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 256..265
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT TRANSMEM 273..285
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q04IN8"
FT MOTIF 427..437
FT /note="Conserved undecapeptide"
FT /evidence="ECO:0000305"
FT MOTIF 459..460
FT /note="Cholesterol binding"
FT /evidence="ECO:0000250|UniProtKB:P0C2E9"
SQ SEQUENCE 471 AA; 52899 MW; 966AF46FE2EA5792 CRC64;
MANKAVNDFI LAMNYDKKKL LTHQGESIEN RFIKEGNQLP DEFVVIERKK RSLSTNTSDI
SVTATNDSRL YPGALLVVDE TLLENNPTLL AVDRAPMTYS IDLPGLASSD SFLQVEDPSN
SSVRGAVNDL LAKWHQDYGQ VNNVPARMQY EKITAHSMEQ LKVKFGSDFE KTGNSLDIDF
NSVHSGEKQI QIVNFKQIYY TVSVDAVKNP GDVFQDTVTV EDLKQRGISA ERPLVYISSV
AYGRQVYLKL ETTSKSDEVE AAFEALIKGV KVAPQTEWKQ ILDNTEVKAV ILGGDPSSGA
RVVTGKVDMV EDLIQEGSRF TADHPGLPIS YTTSFLRDNV VATFQNSTDY VETKVTAYRN
GDLLLDHSGA YVAQYYITWD ELSYDHQGKE VLTPKAWDRN GQDLTAHFTT SIPLKGNVRN
LSVKIRECTG LAWEWWRTVY EKTDLPLVRK RTISIWGTTL YPQVEDKVEN D
