KTXA_KLULA
ID KTXA_KLULA Reviewed; 1146 AA.
AC P09805;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Killer toxin subunits alpha/beta;
DE AltName: Full=RF2 protein;
DE Contains:
DE RecName: Full=Killer toxin subunit alpha;
DE Contains:
DE RecName: Full=Killer toxin subunit beta;
DE EC=3.2.1.14;
DE AltName: Full=Endochitinase;
DE Flags: Precursor;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OG Plasmid pGKl-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX DOI=10.1007/BF00436963;
RA Sor F., Fukuhara H.;
RT "Structure of a linear plasmid of the yeast Kluyveromyces lactis; compact
RT organization of the killer genome.";
RL Curr. Genet. 9:147-155(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=6473099; DOI=10.1093/nar/12.15.6011;
RA Stark M.J.R., Mileham A.J., Romanos M.A., Boyd A.;
RT "Nucleotide sequence and transcription analysis of a linear DNA plasmid
RT associated with the killer character of the yeast Kluyveromyces lactis.";
RL Nucleic Acids Res. 12:6011-6030(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 52735 / 2105-1D;
RX PubMed=6387625; DOI=10.1093/nar/12.19.7581;
RA Hishinuma F., Nakamura K., Hirai K., Nishizawa R., Gunge N., Maeda T.;
RT "Cloning and nucleotide sequences of the linear DNA killer plasmids from
RT yeast.";
RL Nucleic Acids Res. 12:7581-7597(1984).
RN [4]
RP IDENTIFICATION OF PROTEIN, AND PROTEIN SEQUENCE OF 30-44 AND 895-916.
RX PubMed=3758030; DOI=10.1002/j.1460-2075.1986.tb04455.x;
RA Stark M.J.R., Boyd A.;
RT "The killer toxin of Kluyveromyces lactis: characterization of the toxin
RT subunits and identification of the genes which encode them.";
RL EMBO J. 5:1995-2002(1986).
RN [5]
RP SIMILARITY TO CHITINASE OF ALPHA-SUBUNIT.
RX PubMed=2342564; DOI=10.1038/345299b0;
RA Bradshaw H.D. Jr.;
RT "Killer toxins.";
RL Nature 345:299-299(1990).
RN [6]
RP CHITINASE ACTIVITY OF ALPHA-SUBUNIT.
RX PubMed=2070799; DOI=10.1111/j.1432-1033.1991.tb16147.x;
RA Butler A.R., O'Donnell R.W., Martin V.J., Gooday G.W., Stark M.J.R.;
RT "Kluyveromyces lactis toxin has an essential chitinase activity.";
RL Eur. J. Biochem. 199:483-488(1991).
CC -!- FUNCTION: The alpha subunit is a potent exochitinase. Along with the
CC beta subunit it plays a role in the initial interaction of the toxin
CC with sensitive cells and allow the gamma subunit (the active toxin) to
CC gain entry into the cell.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- SUBUNIT: The killer toxin is composed of three subunits: alpha, beta
CC and gamma.
CC -!- PTM: RF2 is potentially split by membrane-bound basic amino acid-
CC specific peptidase to yield the alpha and beta subunits.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01258}.
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DR EMBL; X07127; CAA30137.1; -; Genomic_DNA.
DR EMBL; X00762; CAA25334.1; -; Genomic_DNA.
DR EMBL; X01095; CAA25569.1; -; Genomic_DNA.
DR PIR; S07915; S07915.
DR AlphaFoldDB; P09805; -.
DR SMR; P09805; -.
DR STRING; 284590.P09805; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18A_KLULA; -.
DR PRIDE; P09805; -.
DR Proteomes; UP000000598; Plasmid pGKL1.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; -; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR SUPFAM; SSF57016; SSF57016; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Plasmid;
KW Polysaccharide degradation; Reference proteome; Repeat; Signal; Toxin.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..29
FT /evidence="ECO:0000255"
FT /id="PRO_0000011938"
FT CHAIN 30..892
FT /note="Killer toxin subunit alpha"
FT /evidence="ECO:0000305"
FT /id="PRO_0000011939"
FT CHAIN 895..1146
FT /note="Killer toxin subunit beta"
FT /evidence="ECO:0000305"
FT /id="PRO_0000011940"
FT DOMAIN 205..234
FT /note="LysM 1"
FT DOMAIN 254..303
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 316..372
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 383..735
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 495
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 424
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 447..450
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 496
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 562..565
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 707
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 876
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 319..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 332..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 337..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 366..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1146 AA; 128937 MW; BF4B1764EB465DE6 CRC64;
MNIFYIFLFL LSFVQGLEHT HRRGSLVKRA VCYDTDQVPL NIFFGYNRAD KTDSNKNMAL
NIFNVFRGFL AGEGGESFYN SNGNVYGFMW VGSMVHNRGF KDNILPIMEN EVKNYGIPKT
LYLEYDGGGD PMKSFGIILD TTSRDTVVKA AKLWSQGKKL NSYEGSKNYQ ATACYLSYAY
RKPIVNDNFV GTCDYFTLES GKTPADQSGI NGESLQGYNP NLDFSKLSAG QPICKTIGNP
PNFKPSKNSD GSCKTYKVSS GESCSSIAVK YYPLSLNDIE NYNKGNYGWK GCSSLQKDYN
LCVSDGSAPR PVSNPIAECG PLAPGEKYNA KCPLNACCSE FGFCGLTKDY CDKKSSTTGA
PGTDGCFSNC GYGSTSNVKS STFKKIAYWL DAKDKLAMDP KNIPNGPYDI LHYAFVNINS
DFSIDDSAFS KSAFLKVTSS KKIPSFGGWD FSTSPSTYTI FRNAVKTDQN RNTFANNLIN
FMNKYNLDGI DLDWEYPGAP DIPDIPADDS SSGSNYLTFL KLLKGKMPSG KTLSIAIPSS
YWYLKNFPIS DIQNTVDYMV YMTYDIHGIW EYGKANSYIN CHTPRKEIED AIKMLDKAGV
KFNKVFGGVA NYGRSYKMVN TNCYNYGCGF QREGGNSRDM TNTPGVLSDS EIIDIDSSDK
KNDRWVDTNT DCIFMKYDGN SVVSWPKSRY DLEDMFKNYG FAGTSLWAAN YFKHDEWKND
EDDNNDDTED PFDEENVYFD VYDCKNKAGY DLDNPVYGCR LETAINIIIW NGTESVNTVL
NILNDYDNYI KYYEALTRAH YDSVMEKYEK WLFEEDGYYT YYTDVDGDDI IITPPDKKKR
DYIQEKYSFE KEFMMSQNMT ELTEIKVNKT INFMLNGTSL AVKEYNNEKV LYKRGDIPPP
GSNNRLIRNS IILDKDKEAA IASFKQYSGI ELSKDSFVQR DKDKKFDLNG KHYTFMHSTI
LNAIVLFPNV LTNIDSDYIH HISDLIEQAH NSLGNESPDN IYEVLESVVV FMSVSEIADY
TYTEGKKIKE KYDKMKKTMI VGIILGIIGG LSLFLGPIGI ATSVLADFAL LGADAAINGE
LNPSDLAFAL AGLFLPVFAS LGKTFKFAEA LQKININKSK NFDNLNEFEK IRFFRSKLGK
VKMCGS
