LKTA_MANGL
ID LKTA_MANGL Reviewed; 953 AA.
AC Q9ETX2; Q9EV23; Q9EV24; Q9EV25; Q9EV26;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Leukotoxin;
DE Short=Lkt;
GN Name=lktA;
OS Mannheimia glucosida.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=85401;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype A11 / PH240, Serotype A11 / PH344, Serotype A11 / PH498,
RC Serotype UG3 / PH290, Serotype UG3 / PH496, and Serotype UG3 / PH574;
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 week 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; AF314517; AAG40301.1; -; Genomic_DNA.
DR EMBL; AF314518; AAG40302.1; -; Genomic_DNA.
DR EMBL; AF314519; AAG40303.1; -; Genomic_DNA.
DR EMBL; AF314520; AAG40304.1; -; Genomic_DNA.
DR EMBL; AF314521; AAG40305.1; -; Genomic_DNA.
DR EMBL; AF314522; AAG40306.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ETX2; -.
DR SMR; Q9ETX2; -.
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; 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; 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_0000196218"
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 30..36
FT /note="Missing (in strain: PH574)"
FT VARIANT 126
FT /note="G -> S (in strain: PH496)"
FT VARIANT 550
FT /note="V -> I (in strain: PH290)"
FT VARIANT 656
FT /note="Q -> R (in strain: PH240)"
FT VARIANT 711
FT /note="V -> I (in strain: PH240)"
FT VARIANT 831
FT /note="R -> K (in strain: PH496)"
FT VARIANT 879
FT /note="D -> E (in strain: PH240)"
FT VARIANT 882
FT /note="A -> E (in strain: PH240)"
FT VARIANT 885
FT /note="N -> K (in strain: PH240)"
FT VARIANT 889..895
FT /note="TQDELSK -> DKSDLSQ (in strain: PH240)"
SQ SEQUENCE 953 AA; 102136 MW; 70DB354157F5881E CRC64;
MGNKLTNIST NLKSSWLTAK SGLNRTGQSL AKAGQSLKTG AKKIILYIPK DYQYDTEKGN
GLQDLVKAAE 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
VEWEKNNHGK NYFENGYDAR YLANLQDNMK FLLNLNKELQ AERVIAITQQ QWDNNIGDLA
GISRLGEKVL SGKAYVDAFE EGKHLKADKL VQLDSANGII DVSNSGKAKT QHILFRTPLL
TPGTEHRERV QTGKYEYITK LNINRVDSWK ITDGAASSTF DLTNVVQRIG IELDNAGNVT
KTKETKIVAK LGAGDDNVFV GSGTTEIDGG EGYDRVHYSR GNYGALTIDA TKETEQGSYT
VNRFVETGKA LHEVTSTHTA LVGNREEKIE YRHSNNQHHA GYYTKDTLKA VEEIIGTSHN
DIFKGSKFND AFNGGDGVDT IDGNDGNDRL FGGKGDDIID GGNGDDFIDG GKGNDLLHGG
KGDDIFVHRQ GDGNDIITDS DGNDKLSFSD SNLKDLTFEK VKHNLVITNS RKEKVTIQDW
FREADFAKEV RNYKATKDEK IEEIIGQNGE RITSKQVDDL IAKGNGKITQ DELSKVVDNY
ELLKHSKNVT NSLDKLISSA SAFTSSNDSR NVLVAPTSML DQSLSSLQFA RAA
