ID LKA16_MANHA Reviewed; 953 AA.
AC Q9EV32;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 13-SEP-2023, entry version 84.
DE RecName: Full=Leukotoxin;
DE Short=Lkt;
GN Name=lktA;
OS Mannheimia haemolytica (Pasteurella haemolytica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=75985;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype A16 / PH706;
RX PubMed=11157953; DOI=10.1128/jb.183.4.1394-1404.2001;
RA Davies R.L., Whittam T.S., Selander R.K.;
RT "Sequence diversity and molecular evolution of the leukotoxin (lktA) gene
RT in bovine and ovine strains of Mannheimia (Pasteurella) haemolytica.";
RL J. Bacteriol. 183:1394-1404(2001).
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 is a major contributor to the pathogenesis of lung injury in
CC ovine pneumonic pasteurellosis. It has also weak hemolytic activity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF314509; AAG40293.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9EV32; -.
DR SMR; Q9EV32; -.
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:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR013550; RTX_C.
DR InterPro; IPR018504; RTX_pore_form.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR NCBIfam; NF033943; RTX_toxin; 1.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF00353; HemolysinCabind; 2.
DR Pfam; PF02382; RTX; 1.
DR Pfam; PF08339; RTX_C; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 4.
PE 3: Inferred from homology;
KW Calcium; Cytolysis; Hemolysis; Host cell membrane; Host membrane;
KW Lipoprotein; Membrane; Repeat; Secreted; Toxin; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..953
FT /note="Leukotoxin"
FT /id="PRO_0000196233"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 715..732
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 733..750
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 751..768
FT /note="Hemolysin-type calcium-binding 3"
FT REPEAT 769..786
FT /note="Hemolysin-type calcium-binding 4"
FT REPEAT 789..806
FT /note="Hemolysin-type calcium-binding 5"
SQ SEQUENCE 953 AA; 102079 MW; EF425243C8741EE4 CRC64;
MGNKLTNIST NLKSSWLTAK SGLNRTGQSL AKAGQSLKTG AKKIILYIPK DYQYDTEKGN
GLQDLVKAAQ ELGIEVQKEE GNDIAKAQTS LGTIQNVLGL TERGIVLSAP QLDKLLQKTK
VGQAIGSAEN LTKGFSNAKT VLSGIQSILG SVLAGMDLDE ALQKNSNELT LAKAGLELTN
SLIENIANSV KTLDAFGDQI NQLGSKLQNV KGLSSLGDKL KGLSGFDKTS LGLDVVSGLL
SGATAALVLA DKNASTSRKV GAGFELANQV VGNITKAVSS YILAQRVAAG LSSTGPVAAL
IASTVSLAIS PLAFAGIADK FNHAKSLESY AERFKKLGYD GDNLLAEYQR GTGTIDASVT
AINTALAAIA GGVSAAAAGS VIASPIALLV SGITGVISTI LQYSKQAMFE HVANKIHNKI
VEWEKNNGGK NYFENGYDAR YLANLQDNMK FLLNLNKELQ AERVIAITQQ QWDSNIGDLA
GISRLGEKVL SGKAYVDAFE EGQHLKADKL VQLDSAKGII DVSNTGEAKT QHILFRTPLL
TPGTEKRERV QTGKYEYITK LHINRVDSWK ITDGAASSTF DLTNVVQRIG IELDNAGNVT
KTKETKIIAK LGEGDDNVFV GSGTTEIDGG EGYDRVHYSR GNYGALTIDA TKETEQGSYT
VNRFVESGKA LHEVTSTHTA LVGNREEKIE YRHSNNQHHA GYYTKDTLKA VEEIIGTSHN
DIFKGSKFND AFNGGDGVDT IDGNDGNDRL FGGKGDDIID GGNGDDFIDG GKGNDLLHGG
KGDDIFVHRQ GDGNDSITES EGNDKLSFSD SNLKDLTFEK VNHHLVITNT KQEKVTIQNW
FREAEFAKTI QNYVATRDDK IEEIIGQNGE RITSKQVDEL IEKGNGKIAQ SELTKVVDNY
QLLKYSRDAS NSLDKLISSA SAFTSSNDSR NVLASPTSML DPSLSSIQFA RAA
//
