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P09805

- KTXA_KLULA

UniProt

P09805 - KTXA_KLULA

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Protein

Killer toxin subunits alpha/beta

Gene
N/A
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

The alpha subunit is a potent exochitinase. Along with the beta subunit it plays a role in the initial interaction of the toxin with sensitive cells and allow the gamma subunit (the active toxin) to gain entry into the cell.

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei495 – 4951Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. chitinase activity Source: UniProtKB-EC
  2. chitin binding Source: UniProtKB-KW

GO - Biological processi

  1. chitin catabolic process Source: UniProtKB-KW
  2. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Toxin

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
CBM50. Carbohydrate-Binding Module Family 50.
GH18. Glycoside Hydrolase Family 18.
mycoCLAPiCHI18A_KLULA.

Names & Taxonomyi

Protein namesi
Recommended name:
Killer toxin subunits alpha/beta
Alternative name(s):
RF2 protein
Cleaved into the following 2 chains:
Encoded oniPlasmid pGKl-10 Publication
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Plasmid pGKL1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 2912Sequence AnalysisPRO_0000011938Add
BLAST
Chaini30 – 892863Killer toxin subunit alphaCuratedPRO_0000011939Add
BLAST
Chaini895 – 1146252Killer toxin subunit betaCuratedPRO_0000011940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi319 ↔ 338PROSITE-ProRule annotation
Disulfide bondi332 ↔ 344PROSITE-ProRule annotation
Disulfide bondi337 ↔ 351PROSITE-ProRule annotation
Disulfide bondi366 ↔ 370PROSITE-ProRule annotation
Glycosylationi771 – 7711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi858 – 8581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi868 – 8681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi876 – 8761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi995 – 9951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1082 – 10821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1117 – 11171N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

RF2 is potentially split by membrane-bound basic amino acid-specific peptidase to yield the alpha and beta subunits.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

The killer toxin is composed of three subunits: alpha, beta and gamma.

Structurei

3D structure databases

ProteinModelPortaliP09805.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati205 – 23430LysM 1Add
BLAST
Repeati256 – 28530LysM 2Add
BLAST
Domaini316 – 37257Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation
Contains 2 LysM repeats.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018392. LysM_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
PF01476. LysM. 1 hit.
[Graphical view]
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
SM00636. Glyco_18. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54106. SSF54106. 1 hit.
SSF54556. SSF54556. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09805-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIFYIFLFL LSFVQGLEHT HRRGSLVKRA VCYDTDQVPL NIFFGYNRAD
60 70 80 90 100
KTDSNKNMAL NIFNVFRGFL AGEGGESFYN SNGNVYGFMW VGSMVHNRGF
110 120 130 140 150
KDNILPIMEN EVKNYGIPKT LYLEYDGGGD PMKSFGIILD TTSRDTVVKA
160 170 180 190 200
AKLWSQGKKL NSYEGSKNYQ ATACYLSYAY RKPIVNDNFV GTCDYFTLES
210 220 230 240 250
GKTPADQSGI NGESLQGYNP NLDFSKLSAG QPICKTIGNP PNFKPSKNSD
260 270 280 290 300
GSCKTYKVSS GESCSSIAVK YYPLSLNDIE NYNKGNYGWK GCSSLQKDYN
310 320 330 340 350
LCVSDGSAPR PVSNPIAECG PLAPGEKYNA KCPLNACCSE FGFCGLTKDY
360 370 380 390 400
CDKKSSTTGA PGTDGCFSNC GYGSTSNVKS STFKKIAYWL DAKDKLAMDP
410 420 430 440 450
KNIPNGPYDI LHYAFVNINS DFSIDDSAFS KSAFLKVTSS KKIPSFGGWD
460 470 480 490 500
FSTSPSTYTI FRNAVKTDQN RNTFANNLIN FMNKYNLDGI DLDWEYPGAP
510 520 530 540 550
DIPDIPADDS SSGSNYLTFL KLLKGKMPSG KTLSIAIPSS YWYLKNFPIS
560 570 580 590 600
DIQNTVDYMV YMTYDIHGIW EYGKANSYIN CHTPRKEIED AIKMLDKAGV
610 620 630 640 650
KFNKVFGGVA NYGRSYKMVN TNCYNYGCGF QREGGNSRDM TNTPGVLSDS
660 670 680 690 700
EIIDIDSSDK KNDRWVDTNT DCIFMKYDGN SVVSWPKSRY DLEDMFKNYG
710 720 730 740 750
FAGTSLWAAN YFKHDEWKND EDDNNDDTED PFDEENVYFD VYDCKNKAGY
760 770 780 790 800
DLDNPVYGCR LETAINIIIW NGTESVNTVL NILNDYDNYI KYYEALTRAH
810 820 830 840 850
YDSVMEKYEK WLFEEDGYYT YYTDVDGDDI IITPPDKKKR DYIQEKYSFE
860 870 880 890 900
KEFMMSQNMT ELTEIKVNKT INFMLNGTSL AVKEYNNEKV LYKRGDIPPP
910 920 930 940 950
GSNNRLIRNS IILDKDKEAA IASFKQYSGI ELSKDSFVQR DKDKKFDLNG
960 970 980 990 1000
KHYTFMHSTI LNAIVLFPNV LTNIDSDYIH HISDLIEQAH NSLGNESPDN
1010 1020 1030 1040 1050
IYEVLESVVV FMSVSEIADY TYTEGKKIKE KYDKMKKTMI VGIILGIIGG
1060 1070 1080 1090 1100
LSLFLGPIGI ATSVLADFAL LGADAAINGE LNPSDLAFAL AGLFLPVFAS
1110 1120 1130 1140
LGKTFKFAEA LQKININKSK NFDNLNEFEK IRFFRSKLGK VKMCGS
Length:1,146
Mass (Da):128,937
Last modified:July 1, 1989 - v1
Checksum:iBF4B1764EB465DE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07127 Genomic DNA. Translation: CAA30137.1.
X00762 Genomic DNA. Translation: CAA25334.1.
X01095 Genomic DNA. Translation: CAA25569.1.
PIRiS07915.
RefSeqiYP_001648054.1. NC_010185.1.
YP_001648058.1. NC_010186.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07127 Genomic DNA. Translation: CAA30137.1 .
X00762 Genomic DNA. Translation: CAA25334.1 .
X01095 Genomic DNA. Translation: CAA25569.1 .
PIRi S07915.
RefSeqi YP_001648054.1. NC_010185.1.
YP_001648058.1. NC_010186.1.

3D structure databases

ProteinModelPortali P09805.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM18. Carbohydrate-Binding Module Family 18.
CBM50. Carbohydrate-Binding Module Family 50.
GH18. Glycoside Hydrolase Family 18.
mycoCLAPi CHI18A_KLULA.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
3.30.60.10. 1 hit.
InterProi IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018392. LysM_dom.
[Graphical view ]
Pfami PF00187. Chitin_bind_1. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
PF01476. LysM. 1 hit.
[Graphical view ]
ProDomi PD000609. Chitin_bd_1. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00270. ChtBD1. 1 hit.
SM00636. Glyco_18. 1 hit.
SM00257. LysM. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
SSF54106. SSF54106. 1 hit.
SSF54556. SSF54556. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEi PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS01095. CHITINASE_18. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Structure of a linear plasmid of the yeast Kluyveromyces lactis; compact organization of the killer genome."
    Sor F., Fukuhara H.
    Curr. Genet. 9:147-155(1985)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 76492 / CBS 2359/152 / CLIB 210.
  2. "Nucleotide sequence and transcription analysis of a linear DNA plasmid associated with the killer character of the yeast Kluyveromyces lactis."
    Stark M.J.R., Mileham A.J., Romanos M.A., Boyd A.
    Nucleic Acids Res. 12:6011-6030(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
  3. "Cloning and nucleotide sequences of the linear DNA killer plasmids from yeast."
    Hishinuma F., Nakamura K., Hirai K., Nishizawa R., Gunge N., Maeda T.
    Nucleic Acids Res. 12:7581-7597(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 52735 / 2105-1D.
  4. "The killer toxin of Kluyveromyces lactis: characterization of the toxin subunits and identification of the genes which encode them."
    Stark M.J.R., Boyd A.
    EMBO J. 5:1995-2002(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROTEIN, PROTEIN SEQUENCE OF 30-44 AND 895-916.
  5. Cited for: SIMILARITY TO CHITINASE OF ALPHA-SUBUNIT.
  6. "Kluyveromyces lactis toxin has an essential chitinase activity."
    Butler A.R., O'Donnell R.W., Martin V.J., Gooday G.W., Stark M.J.R.
    Eur. J. Biochem. 199:483-488(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHITINASE ACTIVITY OF ALPHA-SUBUNIT.

Entry informationi

Entry nameiKTXA_KLULA
AccessioniPrimary (citable) accession number: P09805
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 1, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3