LKTA_BIBTR
ID LKTA_BIBTR Reviewed; 955 AA.
AC P55117; P55116; Q51865; Q51866; Q51867; Q51868; Q798V3; Q798V4; Q9EUD4;
AC Q9EV22;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Leukotoxin;
DE Short=Lkt;
GN Name=lktA;
OS Bibersteinia trehalosi (Pasteurella trehalosi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Bibersteinia.
OX NCBI_TaxID=47735;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype T3;
RX PubMed=8225575; DOI=10.1128/iai.61.12.5001-5007.1993;
RA Burrows L.L., Olah-Winfield E., Lo R.Y.C.;
RT "Molecular analysis of the leukotoxin determinants from Pasteurella
RT haemolytica serotypes 1 to 16.";
RL Infect. Immun. 61:5001-5007(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype T10 / 152/92;
RX PubMed=8828217; DOI=10.1099/00221287-142-9-2499;
RA Lainson F.A., Murray J., Davies R.C., Donachie W.;
RT "Characterization of epitopes involved in the neutralization of Pasteurella
RT haemolytica serotype A1 leukotoxin.";
RL Microbiology 142:2499-2507(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype T10 / PH252, Serotype T15 / PH254, Serotype T3 / PH68, and
RC Serotype T4 / PH246;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 723-955.
RC STRAIN=Serotype T10;
RA Lainson F.A., Aitchison K.D., Donachie W.;
RT "DNA sequence of the carboxy terminal end of leukotoxin A from the T10
RT serotype of Pasteurella haemolytica.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 745-955.
RC STRAIN=Serotype T3;
RA Lainson F.A., Aitchison K.D., Donachie W.;
RT "DNA sequence of the carboxy terminal end of leukotoxin A from the T3
RT serotype of Pasteurella haemolytica.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 748-955.
RC STRAIN=Serotype T4;
RA Lainson F.A., Aitchison K.D., Donachie W.;
RT "DNA sequence of the carboxy terminal end of leukotoxin A from the T4
RT serotype of Pasteurella haemolytica.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 756-955.
RC STRAIN=Serotype T15;
RA Lainson F.A., Aitchison K.D., Donachie W.;
RT "DNA sequence of the carboxy terminal end of leukotoxin A from the T15
RT serotype of Pasteurella haemolytica.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
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; U01216; AAB36691.1; -; Unassigned_DNA.
DR EMBL; Z26247; CAA81206.1; -; Genomic_DNA.
DR EMBL; AF314523; AAG40307.1; -; Genomic_DNA.
DR EMBL; AF314524; AAG40308.1; -; Genomic_DNA.
DR EMBL; AF314525; AAG40309.1; -; Genomic_DNA.
DR EMBL; AF314526; AAG40310.1; -; Genomic_DNA.
DR EMBL; Z22887; CAA80501.1; -; Genomic_DNA.
DR EMBL; Z22884; CAA80498.1; -; Genomic_DNA.
DR EMBL; Z22885; CAA80499.1; -; Genomic_DNA.
DR EMBL; Z22886; CAA80500.1; -; Genomic_DNA.
DR PIR; S34238; S34238.
DR PIR; S37145; A35254.
DR AlphaFoldDB; P55117; -.
DR SMR; P55117; -.
DR STRING; 1263831.F543_6970; -.
DR TCDB; 1.C.11.1.1; the pore-forming rtx toxin (rtx-toxin) family.
DR PRIDE; P55117; -.
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..955
FT /note="Leukotoxin"
FT /id="PRO_0000196235"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 7..8
FT /note="Missing (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="A -> V (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="I -> T (in Ref. 2; CAA81206)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..153
FT /note="SILGS -> GNSRT (in Ref. 2; CAA81206)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="D -> H (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..240
FT /note="ISG -> KSR (in Ref. 2; CAA81206)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="G -> R (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="L -> V (in Ref. 2; CAA81206)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="S -> T (in Ref. 2; CAA81206)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="T -> P (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="V -> G (in Ref. 2; CAA81206)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="D -> H (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="D -> V (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="R -> Q (in Ref. 2, 3; AAG40310, 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="E -> D (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="E -> A (in Ref. 1; AAB36691)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="K -> N (in Ref. 1, 2, 3; AAG40310, 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 891..897
FT /note="DKSDLSQ -> AQSELTK (in Ref. 1, 2, 3; AAG40310, 4 and
FT 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 955 AA; 102128 MW; 074B2E4ADFFF57AA CRC64;
MGTKLTLSTL SNGIRSTLTA TRGGLNRAGQ SLTQAGQTLK NGAKKIILYI PKDYKYDSGS
GNGLQDLVKA AEELGIEVQK EEGNDIAKAQ TSLGTIQNVL GLTERGIVLS APQLDKLLQK
NKVGQALGSS ESIAQNFSQA KTVLSGVQSI LGSVLAGMDL DEALQNESDQ LTLAKAGLEL
TNSLIENIAN SVQTLDAFSE QISQFGSKLQ NVKGLGALGD KLKNIGGLDK AGLGLDVISG
LLSGATAALV LADKDASTAK KVGAGFELAN QVVGNITKAV SSYILAQRVA AGLSSTGPVA
ALIASTVALA ISPLSFAGIA DKFDRAKSLE NYAERFKKLG YEGDSLLAEY QHGTGTIDAS
VTAINTALAA IAGGVSAAAA GSVVASPIAL LVSGITGVIS TILQYSKQAM FEHVANKIHN
KIVEWEKNNG GKNYFENGYD ARYLANLQDN MKFLLNLNKE LQAERVIAIT QQQWDSNIGD
LAGISRLGEK VLSGKAYVDA FEEGQHLKAD KLVQLDSAKG IIDVSNTGEA KTQHILFRTP
LLTPGTEKRE RVQTGKYEYI TKLHINRVDS WQIKDGAASS TFDLTNVVQR IGVELDHAEN
VIKTKETKIV ATLGDGDDNV FVGSGTTEID GGEGYDRVHY SRGNYGALTI DATKETEQGS
YTVNRFVESG KALHEVTSTH TALVGNREEK IEYRHSNNQH HAGYYTKDTL KAVEEIIGTS
HNDIFKGSKF NDAFNGGDGV DTIDGNDGND RLFGGKGDDI IDGGNGDDFI DGGKGNDLLH
GGKGDDIFVH RQGDGNDSIT ESEGNDKLSF SDSNLKDLTF EKVNHHLVIT NTKQEKVTIQ
NWFREAEFAK TIRNYVATRD DKIEEIIGQN GERITSKQVD ELIEKGKGKI DKSDLSQVVD
NYQLLKYSRD ASNSLDKLIS SASAFTSSND SRNVLASPTS MLDPSLSSIQ FARAA
