LUKEV_STAA8
ID LUKEV_STAA8 Reviewed; 306 AA.
AC Q2FXB0;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Leucotoxin LukEv;
DE AltName: Full=Variant of LukE;
DE Flags: Precursor;
GN Name=lukEv; OrderedLocusNames=SAOUHSC_01955;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 27733 / V8;
RX PubMed=12636257; DOI=10.1111/j.1348-0421.2003.tb02789.x;
RA Morinaga N., Kaihou Y., Noda M.;
RT "Purification, cloning and characterization of variant LukE-LukD with
RT strong leukocidal activity of staphylococcal bi-component leukotoxin
RT family.";
RL Microbiol. Immunol. 47:81-90(2003).
RN [3]
RP SIMILARITY TO LUKEV.
RX PubMed=15170101; DOI=10.1271/bbb.68.981;
RA Kaneko J., Kamio Y.;
RT "Bacterial two-component and hetero-heptameric pore-forming cytolytic
RT toxins: structures, pore-forming mechanism, and organization of the
RT genes.";
RL Biosci. Biotechnol. Biochem. 68:981-1003(2004).
CC -!- FUNCTION: Part of a bi-component leucotoxin that acts by forming pores
CC in the membrane of the target cells. The activity of LukEv-LukDv to
CC rabbit leukocytes is similar to that of the Panton-Valentine leucocidin
CC (PVL). LukEv-LukDv is hemolytic to rabbit red blood cells although the
CC activity is only 8% of gamma-hemolysin. {ECO:0000269|PubMed:12636257}.
CC -!- SUBUNIT: Toxicity requires sequential binding and synergistic
CC association of a class S and a class F component which form
CC heterooligomeric complexes (By similarity). LukEv (class S) associates
CC with LukDv (class F). {ECO:0000250, ECO:0000269|PubMed:12636257}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD31016.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000253; ABD31016.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000878802.1; NZ_LS483365.1.
DR RefSeq; YP_500454.1; NC_007795.1.
DR PDB; 3ROH; X-ray; 3.20 A; A=1-306.
DR PDB; 7P8S; X-ray; 1.90 A; A=6-306.
DR PDB; 7P8T; X-ray; 1.46 A; A=6-306.
DR PDB; 7P8U; X-ray; 1.60 A; A=6-306.
DR PDB; 7P8X; X-ray; 1.40 A; A=6-306.
DR PDB; 7P93; X-ray; 1.55 A; A=6-306.
DR PDBsum; 3ROH; -.
DR PDBsum; 7P8S; -.
DR PDBsum; 7P8T; -.
DR PDBsum; 7P8U; -.
DR PDBsum; 7P8X; -.
DR PDBsum; 7P93; -.
DR AlphaFoldDB; Q2FXB0; -.
DR SMR; Q2FXB0; -.
DR STRING; 1280.SAXN108_1857; -.
DR EnsemblBacteria; ABD31016; ABD31016; SAOUHSC_01955.
DR GeneID; 3920900; -.
DR KEGG; sao:SAOUHSC_01955; -.
DR PATRIC; fig|93061.5.peg.1780; -.
DR eggNOG; ENOG5030531; Bacteria.
DR HOGENOM; CLU_075311_0_0_9; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR003963; Bi-component_toxin_staph.
DR InterPro; IPR016183; Leukocidin/Hemolysin_toxin.
DR InterPro; IPR036435; Leukocidin/porin_MspA_sf.
DR Pfam; PF07968; Leukocidin; 1.
DR PRINTS; PR01468; BICOMPNTOXIN.
DR SUPFAM; SSF56959; SSF56959; 1.
DR TIGRFAMs; TIGR01002; hlyII; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Hemolysis; Reference proteome; Secreted; Signal;
KW Toxin; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..306
FT /note="Leucotoxin LukEv"
FT /id="PRO_0000419805"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:3ROH"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 50..61
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 66..78
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 94..109
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:3ROH"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:3ROH"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:3ROH"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3ROH"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3ROH"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 249..268
FT /evidence="ECO:0007829|PDB:3ROH"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 272..294
FT /evidence="ECO:0007829|PDB:3ROH"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:3ROH"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:3ROH"
SQ SEQUENCE 306 AA; 34156 MW; E69B17D565CE1A9B CRC64;
MLAATLSVGL IAPLASPIQE SRANTNIENI GDGAEVIKRT EDVSSKKWGV TQNVQFDFVK
DKKYNKDALI VKMQGFINSR TSFSDVKGSG YELTKRMIWP FQYNIGLTTK DPNVSLINYL
PKNKIETTDV GQTLGYNIGG NFQSAPSIGG NGSFNYSKTI SYTQKSYVSE VDKQNSKSVK
WGVKANEFVT PDGKKSAHDR YLFVQSPNGP TGSAREYFAP DNQLPPLVQS GFNPSFITTL
SHEKGSSDTS EFEISYGRNL DITYATLFPR TGIYAERKHN AFVNRNFVVR YEVNWKTHEI
KVKGHN
