ID   LUKE_STAAU              Reviewed;         314 AA.
AC   O54081;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Leucotoxin LukE;
DE   Flags: Precursor;
GN   Name=lukE;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-46, FUNCTION,
RP   SUBUNIT, INDUCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=Newman;
RX   PubMed=9781679; DOI=10.1016/s0014-5793(98)01130-2;
RA   Gravet A., Colin D.A., Keller D., Giradot R., Monteil H., Prevost G.;
RT   "Characterization of a novel structural member, LukE-LukD, of the bi-
RT   component staphylococcal leucotoxins family.";
RL   FEBS Lett. 436:202-208(1998).
CC   -!- FUNCTION: Part of a bi-component leucotoxin that acts by forming pores
CC       in the membrane of the target cells. LukE-LukD is as effective as the
CC       Panton-Valentine leucocidin (PVL) for inducing dermonecrosis when
CC       injected in the rabbit skin, but not hemolytic and poorly leucotoxic on
CC       human blood cells compared to other leucotoxins expressed by S.aureus.
CC       {ECO:0000269|PubMed:9781679}.
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). LukE (class S) associates
CC       with LukD (class F). LukE can also associate with HlgB. {ECO:0000250,
CC       ECO:0000269|PubMed:9781679}.
CC   -!- INTERACTION:
CC       O54081; P51681: CCR5; Xeno; NbExp=2; IntAct=EBI-16027720, EBI-489374;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9781679}.
CC   -!- INDUCTION: Expressed at the late exponential growth. Is cotranscribed
CC       with lukD. {ECO:0000269|PubMed:9781679}.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR   EMBL; Y13225; CAA73667.1; -; Genomic_DNA.
DR   AlphaFoldDB; O54081; -.
DR   SMR; O54081; -.
DR   DIP; DIP-60119N; -.
DR   IntAct; O54081; 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0051715; P:cytolysis in another organism; IEA:InterPro.
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   Cytolysis; Direct protein sequencing; Secreted; Signal; Toxin; Virulence.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:9781679"
FT   CHAIN           29..314
FT                   /note="Leucotoxin LukE"
FT                   /id="PRO_5000147158"
SQ   SEQUENCE   314 AA;  35243 MW;  E4E9D912AA2115CB CRC64;
     MFKKKMLAAS LSVGLIAPLA SPIQESRANT NIENIGDGAE VIKRTEDVSS KKWGVTQNVQ
     FDFVKDKKYN KDALIVKMQG FINSRTSFSD VKGRGYELTK RLIWPFQYNI GLTTKDPNVS
     LINSITLPKT KIETTDVGQT LGYNIGGNFQ SAPSIGGNGS FNYSKTISYT QKSYVSEVDK
     QNSKSVKWGV KANKFVTPDG KKFAHDRYLF VQSPNGPTGS AREYFAPDNQ LPPLVQSGFN
     PSFITTLSHE KGSKLIRVNL KFSYGRNLDI TYATLFPRTG IYAERKHNAF VNRNFVVRYK
     VNWKTHEIKV KGHN