LKTA_PASSP
ID LKTA_PASSP Reviewed; 947 AA.
AC P55123;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Leukotoxin;
DE AltName: Full=PlLkt;
GN Name=lktA;
OS Pasteurella haemolytica-like sp. (strain 5943B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=53500;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8478098; DOI=10.1128/iai.61.5.2089-2095.1993;
RA Chang Y.-F., Ma D.-P., Shi J., Chengappa M.M.;
RT "Molecular characterization of a leukotoxin gene from a Pasteurella
RT haemolytica-like organism, encoding a new member of the RTX toxin family.";
RL Infect. Immun. 61:2089-2095(1993).
CC -!- FUNCTION: Pasteurella leukotoxins are exotoxins that attack host
CC leukocytes and especially polymorphonuclear cells, by causing cell
CC rupture. The leukotoxin binds to the host LFA-1 integrin and induces a
CC signaling cascade leading to many biological effects, including
CC tyrosine phosphorylation of the CD18 tail, elevation of the
CC intracellular Ca(2+) and lysis of the host cell (By similarity). This
CC leukotoxin kills both BL-3 and pig leukocytes and is not hemolytic.
CC {ECO:0000250, ECO:0000269|PubMed:8478098}.
CC -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The transmembrane domains are believed to be involved in pore
CC formation in target cells. {ECO:0000250}.
CC -!- DOMAIN: The Gly-rich region is probably involved in calcium binding,
CC which is required for target cell-binding and cytolytic activity.
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal domain contains an export signal that is
CC recognized by the ABC transporter complex LktBD. {ECO:0000250}.
CC -!- PTM: Acylated by LktC. The toxin only becomes active when modified (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The lktCABD operon has a complex mosaic structure that
CC has been derived by extensive inter- and intraspecies horizontal DNA
CC transfer and intragenic recombination events.
CC -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.
CC {ECO:0000305}.
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DR EMBL; L12148; AAA16444.1; -; Genomic_DNA.
DR AlphaFoldDB; P55123; -.
DR SMR; P55123; -.
DR PRIDE; P55123; -.
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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; -; 1.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR013550; RTX_C.
DR InterPro; IPR018504; RTX_N.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00353; HemolysinCabind; 3.
DR Pfam; PF02382; RTX; 1.
DR Pfam; PF08339; RTX_C; 1.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; SSF51120; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 4.
PE 3: Inferred from homology;
KW Calcium; Cytolysis; Host cell membrane; Host membrane; Lipoprotein;
KW Membrane; Repeat; Secreted; Toxin; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..947
FT /note="Leukotoxin"
FT /id="PRO_0000196234"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 711..728
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 729..746
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 747..764
FT /note="Hemolysin-type calcium-binding 3"
FT REPEAT 765..782
FT /note="Hemolysin-type calcium-binding 4"
FT REPEAT 784..801
FT /note="Hemolysin-type calcium-binding 5"
SQ SEQUENCE 947 AA; 101560 MW; 9744F06395EF5BED CRC64;
MGKLANISTN LKNSLQSGLH KTGQSLNQAG QSLKAGAKKL ILYIPKDYEY DSGRGNGLQD
LVKAAEDLGI EVQREERNGI ATAQNSLSTI QNILGFSERG VVLSAPQLDK LLQKYKISKA
PGSSENVAKN LGNAQTLLSG IQSILGSVMA GMDLDEILKN KGSELDLAKA GLELTNSLIE
NIANSVQTLD TFSEQISQLG TKLQNVKGLG TLGDKLKNFS GFSKAGLGLE VISGLLSGAT
AALVLADKNA STDRKVGAGF ELANQVVGNI TKAVSSYILA QRVAAGLSNT GPVSALIAST
VALAISPLAF AGIADKFNNA KALESYAERF KKLGYEGDSL LAEYQRGTGT IDASVTAVNT
ALAAISGGVS AAAAGSLVGA PIALLVSGIT GIISTILQYS KQAMFEHVAN KIHDKIVDWE
KKHNGKNYFE NGYDSRYLAD LQDNMRQLQN LNKELQAERV IRITQQQWDN NIGNLAGISR
LGEKVMSGKA YADAFEEGKL IKADTFVQLD SATGVINTSK SDNVKTQHIL FRTPLLTPGV
ENRERIQTGK YEYITKLNIN RVDSWKITDG ATNSTFDLTN VVQRIGIELD HADNVTKTKE
TKIIANLGDG NDDVFIGSGT TEVDGGNGLD RVHYSRGDYG ALTIDATNES VQGSYTVKRF
VETGKALHEV TATQSVLVGS REEKIEYRHS NNTQHAGYYT TDTLKSVEEI IGTSRNDIFK
GSKFDDAFHG GDGVDNIDGN AGNDRLFGGK GFDIIDGGDG DDFIDGGQGD DILHGGKGND
ILCTVKGGND SISDSGGNDR LSFADSNLKD LTFEKVNHHL MITNVKKEKV TIQNWFREAD
YAKTVHNYQA TADEKIEEII GRQGERITSK QIDELIEKGK GKIDQSELER IAESSALLKE
SKFASNSLNK LVSSAGAFAS SNDNRVGLGV PTSLYEHTQS VQFVRAA
