LKA2E_MANHA
ID LKA2E_MANHA Reviewed; 953 AA.
AC Q9EV27; Q9EV28;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Leukotoxin;
DE Short=Lkt;
GN Name=lktA;
OS Mannheimia haemolytica (Pasteurella haemolytica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=75985;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype A2 / PH292, and Serotype A2 / PH392;
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}.
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DR EMBL; AF314515; AAG40299.1; -; Genomic_DNA.
DR EMBL; AF314516; AAG40300.1; -; Genomic_DNA.
DR RefSeq; WP_061888577.1; NZ_VAIO01000006.1.
DR AlphaFoldDB; Q9EV27; -.
DR SMR; Q9EV27; -.
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:0044179; P:hemolysis in another organism; 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; 2.
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; 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_0000196225"
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"
FT VARIANT 140
FT /note="T -> I (in strain: PH392)"
SQ SEQUENCE 953 AA; 102218 MW; 04AB1715B819E571 CRC64;
MGNKLTNIST NLKSSWLTAK SGLNRTGQSL AKAGQSLKTG AKKIILYIPK DYQYDTDKGN
GLQDLVKAAE ELGIEVQKEE SNDIAKAQTS LGTIHNVLGL TERGIVLSAP QLDKLLQKTK
VGQAIGSTEN ITKGFSNAKT VLSGIQSILG SVLAGMDLDE ALQNNSNELT LAKAGLELTN
SLIENIANSV KTLDAFGDQI NQLGSKLQNV KGLSSLGEKL KGLSGFDKTS LGLDIVSGLL
SGATAALVLA DKNASTSRKV GAGFELANQV VGNITKAVSS YILAQRVAAG LSSTGPVAAL
IASTVSLAIS PLSFAGIADK FNHAKSLESY AERFKKLGYD GDNLLAEYQR GTGTIDASVT
AINTALAAIA GGVSAAAAGS VVASPIALLV SGITGVISTI LQYSKQAMFE HVANKIHNKI
VEWEKNNPGK NYFENGYDAR YLANLQDNMK FLLNLNKELQ AERVIAITQQ QWDNNIGDLA
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
