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Protein

Endochitinase

Gene

CTS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Chitinase is required for cell separation during growth of Saccharomyces cerevisiae.

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 sitei157 – 1571Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  • chitin binding Source: UniProtKB-KW
  • endochitinase activity Source: SGD

GO - Biological processi

  • cell separation after cytokinesis Source: SGD
  • cell wall organization Source: UniProtKB-KW
  • chitin catabolic process Source: SGD
  • polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Chitin degradation, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Enzyme and pathway databases

BioCyciYEAST:YLR286C-MONOMER.
BRENDAi3.2.1.14. 984.

Protein family/group databases

CAZyiCBM19. Carbohydrate-Binding Module Family 19.
GH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase (EC:3.2.1.14)
Alternative name(s):
Soluble cell wall protein 2
Gene namesi
Name:CTS1
Synonyms:SCW2
Ordered Locus Names:YLR286C
ORF Names:L8003.13
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR286C.
SGDiS000004276. CTS1.

Subcellular locationi

  • Secreted 1 Publication
  • Secretedcell wall 1 Publication

  • Note: Most of the enzyme is secreted, but a significant amount of chitinase is also found associated with the cell wall through binding of C-terminal domain to chitin.

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • extracellular region Source: SGD
  • fungal-type cell wall Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1293195.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 PublicationsAdd
BLAST
Chaini21 – 562542EndochitinasePRO_0000011936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Extensively glycosylated with a series of short O-linked mannose oligosaccharides ranging in size from Man2 to Man5.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP29029.
PeptideAtlasiP29029.

Interactioni

Protein-protein interaction databases

BioGridi31551. 17 interactions.
MINTiMINT-4495746.

Chemistry

BindingDBiP29029.

Structurei

Secondary structure

1
562
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 358Combined sources
Helixi44 – 485Combined sources
Beta strandi50 – 523Combined sources
Beta strandi54 – 6411Combined sources
Turni65 – 673Combined sources
Helixi72 – 743Combined sources
Helixi87 – 9812Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi110 – 1145Combined sources
Helixi119 – 13315Combined sources
Turni143 – 1464Combined sources
Beta strandi150 – 1556Combined sources
Helixi164 – 17512Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi189 – 1935Combined sources
Turni195 – 1973Combined sources
Helixi198 – 2036Combined sources
Beta strandi207 – 2126Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi219 – 2235Combined sources
Helixi226 – 23510Combined sources
Beta strandi243 – 2519Combined sources
Beta strandi254 – 2574Combined sources
Helixi263 – 27311Combined sources
Beta strandi279 – 2857Combined sources
Helixi287 – 2926Combined sources
Beta strandi294 – 2996Combined sources
Helixi300 – 31112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UY2X-ray1.60A22-315[»]
2UY3X-ray1.90A22-315[»]
2UY4X-ray1.75A22-315[»]
2UY5X-ray1.60A22-315[»]
4TXEX-ray1.80A22-315[»]
ProteinModelPortaliP29029.
SMRiP29029. Positions 25-312.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29029.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 327307CatalyticAdd
BLAST
Regioni481 – 56282Chitin-binding, high affinityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi328 – 480153Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000160027.
InParanoidiP29029.
KOiK01183.
OMAiLATYCES.
OrthoDBiEOG7KSXKZ.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR005089. CBM_fam19.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03427. CBM_19. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P29029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLYIILLF TQFLLLPTDA FDRSANTNIA VYWGQNSAGT QESLATYCES
60 70 80 90 100
SDADIFLLSF LNQFPTLGLN FANACSDTFS DGLLHCTQIA EDIETCQSLG
110 120 130 140 150
KKVLLSLGGA SGSYLFSDDS QAETFAQTLW DTFGEGTGAS ERPFDSAVVD
160 170 180 190 200
GFDFDIENNN EVGYSALATK LRTLFAEGTK QYYLSAAPQC PYPDASVGDL
210 220 230 240 250
LENADIDFAF IQFYNNYCSV SGQFNWDTWL TYAQTVSPNK NIKLFLGLPG
260 270 280 290 300
SASAAGSGYI SDTSLLESTI ADIASSSSFG GIALWDASQA FSNELNGEPY
310 320 330 340 350
VEILKNLLTS ASQTATTTVA TSKTSAASTS SASTSSASTS QKKTTQSTTS
360 370 380 390 400
TQSKSKVTLS PTASSAIKTS ITQTTKTLTS STKTKSSLGT TTTESTLNSV
410 420 430 440 450
AITSMKTTLS SQITSAALVT PQTTTTSIVS SAPIQTAITS TLSPATKSSS
460 470 480 490 500
VVSLQTATTS TLSPTTTSTS SGSTSSGSTS SDSTARTLAK ELNAQYAAGK
510 520 530 540 550
LNGKSTCTEG EIACSADGKF AVCDHSAWVY MECASGTTCY AYDSGDSVYT
560
QCNFSYLESN YF
Length:562
Mass (Da):59,015
Last modified:October 1, 1996 - v2
Checksum:i0ABCEFBF448E1E19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681A → R in AAA34539 (PubMed:1918080).Curated
Sequence conflicti168 – 1681A → R in AAA34538 (PubMed:1918080).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161L → P in strain: DBY939.
Natural varianti23 – 231R → S in strain: DBY939 and SEY6210.
Natural varianti321 – 3211T → S in strain: DBY939.
Natural varianti336 – 3405Missing in strain: DBY939.
Natural varianti399 – 3991S → A in strain: DBY939.
Natural varianti433 – 4342PI → SL in strain: DBY939.
Natural varianti461 – 4611T → K in strain: DBY939.
Natural varianti477 – 4815Missing in strain: DBY939.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74070 Genomic DNA. Translation: AAA34539.1.
M74069 Genomic DNA. Translation: AAA34538.1.
U17243 Genomic DNA. Translation: AAB67331.1.
AY693040 Genomic DNA. Translation: AAT93059.1.
BK006945 Genomic DNA. Translation: DAA09597.1.
PIRiA41035.
B41035.
S50371.
RefSeqiNP_013388.1. NM_001182173.1.

Genome annotation databases

EnsemblFungiiYLR286C; YLR286C; YLR286C.
GeneIDi850992.
KEGGisce:YLR286C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74070 Genomic DNA. Translation: AAA34539.1.
M74069 Genomic DNA. Translation: AAA34538.1.
U17243 Genomic DNA. Translation: AAB67331.1.
AY693040 Genomic DNA. Translation: AAT93059.1.
BK006945 Genomic DNA. Translation: DAA09597.1.
PIRiA41035.
B41035.
S50371.
RefSeqiNP_013388.1. NM_001182173.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UY2X-ray1.60A22-315[»]
2UY3X-ray1.90A22-315[»]
2UY4X-ray1.75A22-315[»]
2UY5X-ray1.60A22-315[»]
4TXEX-ray1.80A22-315[»]
ProteinModelPortaliP29029.
SMRiP29029. Positions 25-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31551. 17 interactions.
MINTiMINT-4495746.

Chemistry

BindingDBiP29029.
ChEMBLiCHEMBL1293195.

Protein family/group databases

CAZyiCBM19. Carbohydrate-Binding Module Family 19.
GH18. Glycoside Hydrolase Family 18.

Proteomic databases

MaxQBiP29029.
PeptideAtlasiP29029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR286C; YLR286C; YLR286C.
GeneIDi850992.
KEGGisce:YLR286C.

Organism-specific databases

EuPathDBiFungiDB:YLR286C.
SGDiS000004276. CTS1.

Phylogenomic databases

HOGENOMiHOG000160027.
InParanoidiP29029.
KOiK01183.
OMAiLATYCES.
OrthoDBiEOG7KSXKZ.

Enzyme and pathway databases

BioCyciYEAST:YLR286C-MONOMER.
BRENDAi3.2.1.14. 984.

Miscellaneous databases

EvolutionaryTraceiP29029.
PROiP29029.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR005089. CBM_fam19.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03427. CBM_19. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Chitinase is required for cell separation during growth of Saccharomyces cerevisiae."
    Kuranda M.J., Robbins P.W.
    J. Biol. Chem. 266:19758-19767(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-38.
    Strain: DBY918 and DBY939.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating."
    Cappellaro C., Mrsa V., Tanner W.
    J. Bacteriol. 180:5030-5037(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-32, SUBCELLULAR LOCATION.
    Strain: ATCC 96099 / S288c / SEY6210.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHIT_YEAST
AccessioniPrimary (citable) accession number: P29029
Secondary accession number(s): D6VYT1, P29028
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6350 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.