LKA2A_MANHA
ID LKA2A_MANHA Reviewed; 953 AA.
AC Q9EV30;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 81.
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 / PH196;
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 bovine 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; AF314512; AAG40296.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9EV30; -.
DR SMR; Q9EV30; -.
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_0000196221"
FT TRANSMEM 229..249
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; 102044 MW; 4E8F11490479A69A CRC64;
MGTRLTTLSN GLKNTLTATK SGLHKAGQSL TQAGSSLKTG AKKIILYIPQ NYQYDTEQGN
GLQDLVKAAE ELGIEVQREE RNDIATAQTS LGTIQTAIGL TERGIVLSAP QIDKLLQKTK
AGQALGSAES IVQNANKAKT VLSGIQSILG SVLAGMDLDE ALQNNSNQHA LAKAGLELTN
SLIENIANSV KTLDEFGEQI SQFGSKLQNI KGLGTLGDKL KNIGGLDKAG LGLDVISGLL
SGATAALVLA DKNASTAKKV GAGFELANQV VGNITKAVSS YILAQRVAAG LSSTGPVAAL
IASTVSLAIS PLAFAGIADK FNHAKSLESY AERFKKLGYD GDNLLAEYQR GTGTIDASVT
AINTALAAIA GGVSAAAAGS VIASPIALLV SGITGVISTI LQYSKQAMFE HVANKIHNKI
VEWEKNNQGK NYFENGYDAR YLANLQDNMK FLLNLNKELQ AERVIAITQQ QWDSNIGDLA
GISRLGEKVI SGKAYVDAFE EGKHIKADKL VQLDSAKGII DVSNTGEAKT QHILFRTPLL
TPGTEKRERV QTGKYEYITK LNINRVDSWQ IKDGAASSTF DLTNVVQRIG IELDHAENVT
KTKETKIVAK LGAGDDNVFV GSGTTEIDGG EGYDRVHYSR GNYGALTIDA TKETVQGSYT
VNRFVETGKA LHEVTSTHTA LVGSREEKIE YRHSNNRQHA GYYTKDTLTT IEEIIGTSHN
DIFRGSKFND AFQGGDGVDT IDGNDGNDRL FGGKGDDIID GGNGDDFIDG GKGNDLLHGG
RGDDIFVHRK GDGNDIISDS DGNDKLSFSD SNLKDLTFEK VKYNLVITNS NKEKVTIQNW
FREADLAKEV HNYKATADEK IEEIIGQNGE RITSKQVDDL IEKGNGKITQ DELSKAVDNY
ELLKHSKNVT NSLDKLISSV SSFTSSNDSR NVLVAPASML DQSLSSLQFA RAA
