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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-JUL-2017, entry version 97.
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:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
InterPro; IPR001343; Hemolysn_Ca-bd.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR013550; RTX_C.
InterPro; IPR018504; RTX_N.
InterPro; IPR003995; RTX_toxin_determinant-A.
InterPro; IPR011049; Serralysin-like_metalloprot_C.
Pfam; PF00353; HemolysinCabind; 6.
Pfam; PF02382; RTX; 1.
Pfam; PF08339; RTX_C; 1.
PRINTS; PR01488; RTXTOXINA.
SUPFAM; SSF51120; SSF51120; 3.
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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