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Leukotoxin (Lkt)

 LTXA_AGGAC              Reviewed;        1055 AA.
P16462; Q43892;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
07-JAN-2015, sequence version 2.
05-DEC-2018, entry version 102.
RecName: Full=Leukotoxin;
Short=Lkt;
Name=ltxA {ECO:0000303|PubMed:8300209};
Synonyms=AaLta {ECO:0000303|PubMed:2670940},
lktA {ECO:0000303|PubMed:2318535};
Aggregatibacter actinomycetemcomitans (Actinobacillus
actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
Pasteurellaceae; Aggregatibacter.
NCBI_TaxID=714;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JP2;
PubMed=2670940;
Lally E.T., Golub E.E., Kieba I.R., Taichman N.S., Rosenbloom J.,
Rosenbloom J.C., Gibson C.W., Demuth D.R.;
"Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene.
Delineation of unique features and comparison to homologous toxins.";
J. Biol. Chem. 264:15451-15456(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JP2;
PubMed=2318535;
Kraig E., Dailey T., Kolodrubetz D.;
"Nucleotide sequence of the leukotoxin gene from Actinobacillus
actinomycetemcomitans: homology to the alpha-hemolysin/leukotoxin gene
family.";
Infect. Immun. 58:920-929(1990).
[3]
FUNCTION.
PubMed=3258584;
Simpson D.L., Berthold P., Taichman N.S.;
"Killing of human myelomonocytic leukemia and lymphocytic cell lines
by Actinobacillus actinomycetemcomitans leukotoxin.";
Infect. Immun. 56:1162-1166(1988).
[4]
SUBCELLULAR LOCATION.
STRAIN=301-b / Serotype a;
PubMed=1937819;
Ohta H., Kato K., Kokeguchi S., Hara H., Fukui K., Murayama Y.;
"Nuclease-sensitive binding of an Actinobacillus actinomycetemcomitans
leukotoxin to the bacterial cell surface.";
Infect. Immun. 59:4599-4605(1991).
[5]
INDUCTION, AND GENE NAME.
STRAIN=652, and JP2;
PubMed=8300209;
Brogan J.M., Lally E.T., Poulsen K., Kilian M., Demuth D.R.;
"Regulation of Actinobacillus actinomycetemcomitans leukotoxin
expression: analysis of the promoter regions of leukotoxic and
minimally leukotoxic strains.";
Infect. Immun. 62:501-508(1994).
[6]
SUBCELLULAR LOCATION.
PubMed=11035711; DOI=10.1128/IAI.68.11.6094-6100.2000;
Kachlany S.C., Fine D.H., Figurski D.H.;
"Secretion of RTX leukotoxin by Actinobacillus
actinomycetemcomitans.";
Infect. Immun. 68:6094-6100(2000).
[7]
FUNCTION AS A HEMOLYSIN, AND DISRUPTION PHENOTYPE.
PubMed=16552030; DOI=10.1128/IAI.74.4.2015-2021.2006;
Balashova N.V., Crosby J.A., Al Ghofaily L., Kachlany S.C.;
"Leukotoxin confers beta-hemolytic activity to Actinobacillus
actinomycetemcomitans.";
Infect. Immun. 74:2015-2021(2006).
[8]
REGULATION BY IRON.
PubMed=17041062; DOI=10.1128/JB.01253-06;
Balashova N.V., Diaz R., Balashov S.V., Crosby J.A., Kachlany S.C.;
"Regulation of Aggregatibacter (Actinobacillus) actinomycetemcomitans
leukotoxin secretion by iron.";
J. Bacteriol. 188:8658-8661(2006).
[9]
INTERACTION WITH SUPEROXIDE DISMUTASE.
PubMed=17635874; DOI=10.1128/IAI.00288-07;
Balashova N.V., Park D.H., Patel J.K., Figurski D.H., Kachlany S.C.;
"Interaction between leukotoxin and Cu,Zn superoxide dismutase in
Aggregatibacter actinomycetemcomitans.";
Infect. Immun. 75:4490-4497(2007).
[10]
FUNCTION, AND INTERACTION WITH HUMAN LFA-1.
PubMed=17635865; DOI=10.1128/IAI.00314-07;
Dileepan T., Kachlany S.C., Balashova N.V., Patel J., Maheswaran S.K.;
"Human CD18 is the functional receptor for Aggregatibacter
actinomycetemcomitans leukotoxin.";
Infect. Immun. 75:4851-4856(2007).
[11]
ACYLATION.
STRAIN=JP2N;
PubMed=19450669; DOI=10.1016/j.gene.2009.05.002;
Balashova N.V., Shah C., Patel J.K., Megalla S., Kachlany S.C.;
"Aggregatibacter actinomycetemcomitans LtxC is required for leukotoxin
activity and initial interaction between toxin and host cells.";
Gene 443:42-47(2009).
[12]
ACYLATION, AND MUTAGENESIS OF LYS-562 AND LYS-687.
PubMed=21729247; DOI=10.1111/j.2041-1014.2011.00617.x;
Fong K.P., Tang H.Y., Brown A.C., Kieba I.R., Speicher D.W.,
Boesze-Battaglia K., Lally E.T.;
"Aggregatibacter actinomycetemcomitans leukotoxin is post-
translationally modified by addition of either saturated or
hydroxylated fatty acyl chains.";
Mol. Oral. Microbiol. 26:262-276(2011).
[13]
FUNCTION, BINDING TO CHOLESTEROL, AND MUTAGENESIS OF TYR-337 AND
TYR-504.
PubMed=23792963; DOI=10.1074/jbc.M113.486654;
Brown A.C., Balashova N.V., Epand R.M., Epand R.F., Bragin A.,
Kachlany S.C., Walters M.J., Du Y., Boesze-Battaglia K., Lally E.T.;
"Aggregatibacter actinomycetemcomitans leukotoxin utilizes a
cholesterol recognition/amino acid consensus site for membrane
association.";
J. Biol. Chem. 288:23607-23621(2013).
-!- FUNCTION: Virulence factor that plays an important role in immune
evasion. Lyses human lymphocytes and monocytes. Binds to the LFA-1
integrin on the surface of the host cell and to cholesterol-
containing membranes, which probably results in large LtxA-LFA-1
clusters in lipid rafts. Shows also beta-hemolytic activity on
certain types of growth media. {ECO:0000269|PubMed:16552030,
ECO:0000269|PubMed:17635865, ECO:0000269|PubMed:23792963,
ECO:0000269|PubMed:3258584}.
-!- SUBUNIT: Interacts specifically with the superoxide dismutase [Cu-
Zn]. This interaction may protect LtxA from reactive oxygen
species and reactive nitrogen species produced by host
inflammatory cells during disease (PubMed:17635874). Interacts
with the human leukocyte adhesion glycoprotein LFA-1 (ITGAL-ITGB2)
(PubMed:17635865). {ECO:0000269|PubMed:17635865,
ECO:0000269|PubMed:17635874}.
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000269|PubMed:1937819}; Peripheral membrane protein
{ECO:0000269|PubMed:1937819}; Extracellular side
{ECO:0000269|PubMed:1937819}. Secreted
{ECO:0000269|PubMed:11035711}. Note=Leukotoxin expressed by the
rough, adherent, clinical isolate CU1000N is cell associated.
However, smooth, nonadherent strains, including Y4, JP2 and
CU1060N, secrete an abundance of leukotoxin into the culture
supernatants during early stages of growth (PubMed:11035711).
Secretion is inhibited by free iron (PubMed:17041062).
{ECO:0000269|PubMed:11035711, ECO:0000269|PubMed:17041062}.
-!- INDUCTION: Levels of toxin expression vary greatly among strains.
Highly leukotoxic strains (JP2-type strains) produce more LtxA
protein and ltx mRNA than minimally leukotoxic strains (652-type
strains). Variations are probably due to different types of
promoters (PubMed:8300209). Expression is not affected by iron
(PubMed:17041062). {ECO:0000269|PubMed:17041062,
ECO:0000269|PubMed:8300209}.
-!- DOMAIN: The Gly-rich region is probably involved in binding
calcium, which is required for target cell-binding or cytolytic
activity. {ECO:0000250}.
-!- PTM: Acylated at Lys-562 and Lys-687 by LtxC. This modification is
required for full activity. Isolated methyl esters contain
palmitoyl and palmitolyl fatty acyl groups with smaller quantities
of myristic and stearic fatty acids. {ECO:0000269|PubMed:19450669,
ECO:0000269|PubMed:21729247}.
-!- DISRUPTION PHENOTYPE: Mutation completely abolishes the beta-
hemolytic activity of A.actinomycetemcomitans.
{ECO:0000269|PubMed:16552030}.
-!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M27399; AAA21922.1; -; Genomic_DNA.
EMBL; X16829; CAA34731.1; -; Genomic_DNA.
PIR; A37205; A37205.
ProteinModelPortal; P16462; -.
SMR; P16462; -.
TCDB; 1.C.11.1.7; the pore-forming rtx toxin (rtx-toxin) family.
PRIDE; P16462; -.
eggNOG; ENOG4105DDI; Bacteria.
eggNOG; COG2931; LUCA.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
Gene3D; 2.150.10.10; -; 2.
InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
InterPro; IPR001343; Hemolysn_Ca-bd.
InterPro; IPR013550; RTX_C.
InterPro; IPR018504; RTX_N.
InterPro; IPR003995; RTX_toxin_determinant-A.
InterPro; IPR011049; Serralysin-like_metalloprot_C.
Pfam; PF00353; HemolysinCabind; 3.
Pfam; PF02382; RTX; 1.
Pfam; PF08339; RTX_C; 1.
PRINTS; PR01488; RTXTOXINA.
SUPFAM; SSF51120; SSF51120; 2.
PROSITE; PS00330; HEMOLYSIN_CALCIUM; 5.
1: Evidence at protein level;
Calcium; Cell outer membrane; Coiled coil; Cytolysis; Hemolysis;
Membrane; Repeat; Secreted; Toxin; Virulence.
CHAIN 1 1055 Leukotoxin.
/FTId=PRO_0000196216.
REPEAT 721 738 Hemolysin-type calcium-binding 1.
REPEAT 739 756 Hemolysin-type calcium-binding 2.
REPEAT 757 774 Hemolysin-type calcium-binding 3.
REPEAT 775 792 Hemolysin-type calcium-binding 4.
REPEAT 793 810 Hemolysin-type calcium-binding 5.
REPEAT 811 828 Hemolysin-type calcium-binding 6.
REPEAT 829 846 Hemolysin-type calcium-binding 7.
REGION 334 340 Cholesterol recognition/amino acid
consensus (CRAC) region.
{ECO:0000269|PubMed:23792963}.
REGION 502 506 Cholesterol recognition/amino acid
consensus (CRAC) region.
{ECO:0000269|PubMed:23792963}.
COILED 11 49 {ECO:0000255}.
MUTAGEN 337 337 Y->P: Loss of cytotoxicity.
{ECO:0000269|PubMed:23792963}.
MUTAGEN 504 504 Y->P: Decreases cytotoxicity.
{ECO:0000269|PubMed:23792963}.
MUTAGEN 562 562 K->R: Loss of cytotoxicity.
{ECO:0000269|PubMed:21729247}.
MUTAGEN 687 687 K->R: Loss of cytotoxicity.
{ECO:0000269|PubMed:21729247}.
CONFLICT 240 240 L -> Y (in Ref. 1; AAA21922).
{ECO:0000305}.
CONFLICT 260 260 D -> H (in Ref. 1; AAA21922).
{ECO:0000305}.
CONFLICT 336 336 E -> A (in Ref. 1; AAA21922).
{ECO:0000305}.
CONFLICT 416 416 F -> S (in Ref. 1; AAA21922).
{ECO:0000305}.
CONFLICT 439 439 F -> S (in Ref. 1; AAA21922).
{ECO:0000305}.
CONFLICT 724 724 T -> N (in Ref. 1; AAA21922).
{ECO:0000305}.
CONFLICT 927 1055 RARLKRQFELQRGKVDKSLNNKVEEIIGKDGERITSQDIDN
LFDKSGNKKTISPQELAGLIKNKGKSSSLMSSSRSSSMLTQ
KSGLSNDISRIISATSGFGSSGKALSASPLQTNNNFNSYAN
SLATTA -> VHDLRDNLSYSEVKSTNHSIIKLKKLSVKMG
SGLLRKTLIIFLIRVGTKRQFHLKSLPDLLRIKVSQVALCL
LLVRQVCLHKSPVCQMILVVLFQQPVVLVHPVKRYPLRHCR
PIITLTLTQIR (in Ref. 1; AAA21922).
SEQUENCE 1055 AA; 113854 MW; 5331C396FA76669E CRC64;
MATTTLPNTK QQAAQFANSV ADRAKENIDA AKEQLQKALD KLGKTGKKLT LYIPKNYKKG
NGLTALIKAA QKLGIEVYHE GKDGPALTNG ILNTGKKLLG LTERGLTLFA PELDKWIQGN
KHLSNSVGST GNLTKAIDKV QSVLGTLQAF LNTAFSGMDL DALIKARQNG KNVTDVQLAK
ASLNLINELI GTISSITNNV DTFSKQLNKL GEALGQVKHF GSFGDKLKNL PKLGNLGKGL
GALSGVLSAI SAALLLANKD ADTATKAAAA AELTNKVLGN IGKAITQYLI AQRAAAGLST
TGPVAGLIAS VVSLAISPLS FLGIAKQFDR ARMLEEYSKR FKKFGYNGDS LLGQFYKNTG
IADAAITTIN TVLSAIAAGV GAASAGSLVG APIGLLVSAI TSLISGILDA SKQAVFEHIA
NQLADKIKAW ENKYGKNYFE NGYDARHSAF LEDSLKLFNE LREKYKTENI LSITQQGWDQ
RIGELAGITR NGDRIQSGKA YVDYLKKGEE LAKHSDKFTK QILDPIKGNI DLSGIKGSTT
LTFLNPLLTA GKEERKTRQS GKYEFITELK VKGRTDWKVK GVPNSNGVYD FSNLIQHAVT
RDNKVLEARL IANLGAKDDY VFVGSGSTIV NAGDGYDVVD YSKGRTGALT IDGRNATKAG
QYKVERDLSG TQVLQETVSK QETKRGKVTD LLEYRNYKLD YYYTNKGFKA HDELNSVEEI
IGSTLRDKFY GSKFNDVFHG HDGDDLIYGY DGDDRLYGDN GNDEIHGGQG NDKLYGGAGN
DRLFGEYGNN YLDGGEGDDH LEGGNGSDIL RGGSGNDKLF GNQGDDLLDG GEGDDQLAGG
EGNDIYVYRK EYGHHTITEH SGDKDKLSLA NINLKDVSFE RNGNDLLLKT NNRTAVTFKG
WFSKPNSSAG LDEYQRKLLE YAPEKDRARL KRQFELQRGK VDKSLNNKVE EIIGKDGERI
TSQDIDNLFD KSGNKKTISP QELAGLIKNK GKSSSLMSSS RSSSMLTQKS GLSNDISRII
SATSGFGSSG KALSASPLQT NNNFNSYANS LATTA


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Related Genes :
[ltxA AaLta lktA] Leukotoxin (Lkt)
[ppnP OR1_03385] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[glmU OR1_01412] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[ribA ribB OR37_01047] Multifunctional fusion protein [Includes: GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II); 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12)]
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[nnr nnrD nnrE OR1_02963] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]
[ppnP OR214_03073] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[ppnP OR16_09104] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[ribBA OR1_02316] Riboflavin biosynthesis protein RibBA [Includes: 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12); GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II)]
[nnrE nnrD OR37_00116] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]
[nnrE nnrD OR214_00542] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]
[EP300 P300] Histone acetyltransferase p300 (p300 HAT) (EC 2.3.1.48) (E1A-associated protein p300) (Histone butyryltransferase p300) (EC 2.3.1.-) (Histone crotonyltransferase p300) (EC 2.3.1.-) (Protein propionyltransferase p300) (EC 2.3.1.-)
[OR1F1 OLFMF OR1F10 OR1F4 OR1F5 OR1F6 OR1F7 OR1F8 OR1F9] Olfactory receptor 1F1 (Olfactory receptor 16-35) (OR16-35) (Olfactory receptor 1F10) (Olfactory receptor 1F4) (Olfactory receptor 1F5) (Olfactory receptor 1F6) (Olfactory receptor 1F7) (Olfactory receptor 1F8) (Olfactory receptor 1F9) (Olfactory receptor OR16-4)
[cat-1 NCU08791] Catalase-1 (EC 1.11.1.6)
[glmU OR37_01460] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[glmU OR221_2794] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[murE OR1_01796] UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (Meso-A2pm-adding enzyme) (Meso-diaminopimelate-adding enzyme) (UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase) (UDP-MurNAc-tripeptide synthetase) (UDP-N-acetylmuramyl-tripeptide synthetase)
[frq B13D24.170 NCU02265] Frequency clock protein
[OR1D2 OLFR1] Olfactory receptor 1D2 (Olfactory receptor 17-4) (OR17-4) (Olfactory receptor OR17-6) (Olfactory receptor-like protein HGMP07E)
[glmU OR214_03857] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[OR7D4 OR7D4P] Olfactory receptor 7D4 (OR19-B) (Odorant receptor family subfamily D member 4RT) (Olfactory receptor OR19-7)
[stk-1 bur1 B20D17.070 NCU01435] Serine/threonine-protein kinase bur1 (EC 2.7.11.22) (EC 2.7.11.23) (Serine-threonine kinase 1)
[T 90C4.150 NCU00776] Tyrosinase (EC 1.14.18.1) (Monophenol monooxygenase)
[scon-2 B13M15.090 NCU08563] Probable E3 ubiquitin ligase complex SCF subunit scon-2 (Sulfur controller 2) (SCON2) (Sulfur metabolite repression control protein 2)
[cyt-18 B18P24.070 NCU03030] Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS)
[prs OR1_02395] Ribose-phosphate pyrophosphokinase (RPPK) (EC 2.7.6.1) (5-phospho-D-ribosyl alpha-1-diphosphate) (Phosphoribosyl diphosphate synthase) (Phosphoribosyl pyrophosphate synthase) (P-Rib-PP synthase) (PRPP synthase) (PRPPase)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]

Bibliography :
[30881690] A bovine CD18 signal peptide variant with increased binding activity to leukotoxin.
[30771459] Leukotoxic activity of Fusobacterium necrophorum of cattle origin.
[30683173] Mannheimia haemolytica in bovine respiratory disease: immunogens, potential immunogens, and vaccines.
[28619167] Effect of vaccination against pneumonia on the survival of bighorn sheep (Ovis canadensis) commingled with carrier animals.
[26216418] Acylation Enhances, but Is Not Required for, the Cytotoxic Activity of Mannheimia haemolytica Leukotoxin in Bighorn Sheep.
[24638139] Subcutaneous immunization with inactivated bacterial components and purified protein of Escherichia coli, Fusobacterium necrophorum and Trueperella pyogenes prevents puerperal metritis in Holstein dairy cows.
[24629771] Bighorn sheep × domestic sheep hybrids survive Mannheimia haemolytica challenge in the absence of vaccination.
[23543955] Serum IgG response in calves to the putative pneumonic virulence factor Gs60 of Mannheimia haemolytica A1.
[23050598] Quantitative discrimination of Aggregatibacter actinomycetemcomitans highly leukotoxic JP2 clone from non-JP2 clones in diagnosis of aggressive periodontitis.
[22354029] Mannheimia haemolytica and its leukotoxin cause macrophage extracellular trap formation by bovine macrophages.