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Q9EV32 (LKA16_PASHA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Leukotoxin

Short name=Lkt
Gene names
Name:lktA
OrganismPasteurella haemolytica (Mannheimia haemolytica)
Taxonomic identifier75985 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeMannheimia

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Pasteurella leukotoxins are exotoxins that attack host leukocytes and especially polymorphonuclear cells, by causing cell rupture. The leukotoxin binds to the host LFA-1 integrin and induces a signaling cascade leading to many biological effects, including tyrosine phosphorylation of the CD18 tail, elevation of the intracellular Ca2+ and lysis of the host cell By similarity. This leukotoxin is a major contributor to the pathogenesis of lung injury in ovine pneumonic pasteurellosis. It has also weak hemolytic activity.

Subcellular location

Secreted By similarity. Host cell membrane; Multi-pass membrane protein By similarity.

Domain

The transmembrane domains are believed to be involved in pore formation in target cells By similarity.

The Gly-rich region is probably involved in calcium binding, which is required for target cell-binding and cytolytic activity By similarity.

The C-terminal domain contains an export signal that is recognized by the ABC transporter complex LktBD By similarity.

Post-translational modification

Acylated by LktC. The toxin only becomes active when modified By similarity.

Miscellaneous

The lktCABD operon has a complex mosaic structure that has been derived by extensive inter- and intraspecies horizontal DNA transfer and intragenic recombination events.

Sequence similarities

Belongs to the RTX prokaryotic toxin (TC 1.C.11) family. [View classification]

Contains 5 hemolysin-type calcium-binding repeats.

Ontologies

Keywords
   Biological processCytolysis
Hemolysis
Virulence
   Cellular componentHost cell membrane
Host membrane
Membrane
Secreted
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionToxin
   PTMLipoprotein
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

hemolysis in other organism

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953Leukotoxin
PRO_0000196233

Regions

Transmembrane230 – 25021Helical; Potential
Transmembrane297 – 31721Helical; Potential
Transmembrane359 – 37921Helical; Potential
Transmembrane381 – 40121Helical; Potential
Repeat715 – 73218Hemolysin-type calcium-binding 1
Repeat733 – 75018Hemolysin-type calcium-binding 2
Repeat751 – 76818Hemolysin-type calcium-binding 3
Repeat769 – 78618Hemolysin-type calcium-binding 4
Repeat789 – 80618Hemolysin-type calcium-binding 5

Sequences

Sequence LengthMass (Da)Tools
Q9EV32 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: EF425243C8741EE4

FASTA953102,079
        10         20         30         40         50         60 
MGNKLTNIST NLKSSWLTAK SGLNRTGQSL AKAGQSLKTG AKKIILYIPK DYQYDTEKGN 

        70         80         90        100        110        120 
GLQDLVKAAQ ELGIEVQKEE GNDIAKAQTS LGTIQNVLGL TERGIVLSAP QLDKLLQKTK 

       130        140        150        160        170        180 
VGQAIGSAEN LTKGFSNAKT VLSGIQSILG SVLAGMDLDE ALQKNSNELT LAKAGLELTN 

       190        200        210        220        230        240 
SLIENIANSV KTLDAFGDQI NQLGSKLQNV KGLSSLGDKL KGLSGFDKTS LGLDVVSGLL 

       250        260        270        280        290        300 
SGATAALVLA DKNASTSRKV GAGFELANQV VGNITKAVSS YILAQRVAAG LSSTGPVAAL 

       310        320        330        340        350        360 
IASTVSLAIS PLAFAGIADK FNHAKSLESY AERFKKLGYD GDNLLAEYQR GTGTIDASVT 

       370        380        390        400        410        420 
AINTALAAIA GGVSAAAAGS VIASPIALLV SGITGVISTI LQYSKQAMFE HVANKIHNKI 

       430        440        450        460        470        480 
VEWEKNNGGK NYFENGYDAR YLANLQDNMK FLLNLNKELQ AERVIAITQQ QWDSNIGDLA 

       490        500        510        520        530        540 
GISRLGEKVL SGKAYVDAFE EGQHLKADKL VQLDSAKGII DVSNTGEAKT QHILFRTPLL 

       550        560        570        580        590        600 
TPGTEKRERV QTGKYEYITK LHINRVDSWK ITDGAASSTF DLTNVVQRIG IELDNAGNVT 

       610        620        630        640        650        660 
KTKETKIIAK LGEGDDNVFV GSGTTEIDGG EGYDRVHYSR GNYGALTIDA TKETEQGSYT 

       670        680        690        700        710        720 
VNRFVESGKA LHEVTSTHTA LVGNREEKIE YRHSNNQHHA GYYTKDTLKA VEEIIGTSHN 

       730        740        750        760        770        780 
DIFKGSKFND AFNGGDGVDT IDGNDGNDRL FGGKGDDIID GGNGDDFIDG GKGNDLLHGG 

       790        800        810        820        830        840 
KGDDIFVHRQ GDGNDSITES EGNDKLSFSD SNLKDLTFEK VNHHLVITNT KQEKVTIQNW 

       850        860        870        880        890        900 
FREAEFAKTI QNYVATRDDK IEEIIGQNGE RITSKQVDEL IEKGNGKIAQ SELTKVVDNY 

       910        920        930        940        950 
QLLKYSRDAS NSLDKLISSA SAFTSSNDSR NVLASPTSML DPSLSSIQFA RAA 

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References

[1]"Sequence diversity and molecular evolution of the leukotoxin (lktA) gene in bovine and ovine strains of Mannheimia (Pasteurella) haemolytica."
Davies R.L., Whittam T.S., Selander R.K.
J. Bacteriol. 183:1394-1404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Serotype A16 / PH706.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF314509 Genomic DNA. Translation: AAG40293.1.

3D structure databases

ProteinModelPortalQ9EV32.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR013550. RTX_C.
IPR018504. RTX_N.
IPR003995. RTX_toxin_determinant-A.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamPF00353. HemolysinCabind. 4 hits.
PF02382. RTX. 1 hit.
PF08339. RTX_C. 1 hit.
[Graphical view]
PRINTSPR01488. RTXTOXINA.
SUPFAMSSF51120. Serralysn_like_C. 1 hit.
PROSITEPS00330. HEMOLYSIN_CALCIUM. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLKA16_PASHA
AccessionPrimary (citable) accession number: Q9EV32
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2001
Last modified: April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families