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Protein

Endochitinase B

Gene

CHN50

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Defense against chitin-containing fungal pathogens.

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Pathogenesis-related protein

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Hypersensitive response, Plant defense, Polysaccharide degradation

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Endochitinase B (EC:3.2.1.14)
Short name:
CHN-B
Gene namesi
Name:CHN50
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 317294Endochitinase BPRO_0000005332Add
BLAST
Propeptidei318 – 3247Removed in mature formCuratedPRO_0000005333

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 41PROSITE-ProRule annotation
Disulfide bondi35 ↔ 47PROSITE-ProRule annotation
Disulfide bondi40 ↔ 54PROSITE-ProRule annotation
Disulfide bondi59 ↔ 63PROSITE-ProRule annotation
Modified residuei67 – 6714-hydroxyproline1 Publication
Modified residuei69 – 6914-hydroxyproline1 Publication
Disulfide bondi96 ↔ 158PROSITE-ProRule annotation
Disulfide bondi170 ↔ 178PROSITE-ProRule annotation
Disulfide bondi277 ↔ 309PROSITE-ProRule annotation

Post-translational modificationi

The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein.

Keywords - PTMi

Disulfide bond, Hydroxylation

Expressioni

Inductioni

By ethylene.

Structurei

3D structure databases

ProteinModelPortaliP24091.
SMRiP24091. Positions 24-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 6542Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24091-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLREFTALS SLLFSLLLLS ASAEQCGSQA GGARCASGLC CSKFGWCGNT
60 70 80 90 100
NDYCGPGNCQ SQCPGGPTPP GGGDLGSIIS SSMFDQMLKH RNDNACQGKG
110 120 130 140 150
FYSYNAFINA ARSFPGFGTS GDTTARKREI AAFFAQTSHE TTGGWATAPD
160 170 180 190 200
GPYAWGYCWL REQGSPGDYC TPSGQWPCAP GRKYFGRGPI QISHNYNYGP
210 220 230 240 250
CGRAIGVDLL NNPDLVATDP VISFKSALWF WMTPQSPKPS CHDVIIGRWQ
260 270 280 290 300
PSSADRAANR LPGFGVITNI INGGLECGRG TDSRVQDRIG FYRRYCSILG
310 320
VSPGDNLDCG NQRSFGNGLL VDTM
Length:324
Mass (Da):34,721
Last modified:March 1, 1992 - v1
Checksum:iFA65DC2113B33EB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51599 Genomic DNA. Translation: CAA35945.1.
X64519 Genomic DNA. Translation: CAA45822.1.
M15173 mRNA. Translation: AAA34070.1.
PIRiS20981.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51599 Genomic DNA. Translation: CAA35945.1.
X64519 Genomic DNA. Translation: CAA45822.1.
M15173 mRNA. Translation: AAA34070.1.
PIRiS20981.

3D structure databases

ProteinModelPortaliP24091.
SMRiP24091. Positions 24-315.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFiPIRSF001060. Endochitinase. 1 hit.
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Gene structure and expression of a tobacco endochitinase gene in suspension-cultured tobacco cells."
    Fukuda Y., Ohme M., Shinshi H.
    Plant Mol. Biol. 16:1-10(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Bright Yellow 4.
    Tissue: Leaf.
  2. "The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin."
    van Buuren M., Neuhaus J.-M., Shinshi H., Ryals J., Meins F. Jr.
    Mol. Gen. Genet. 232:460-469(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Havana 425.
    Tissue: Leaf.
  3. "Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin."
    Shinshi H., Mohnen D., Meins F. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 84:89-93(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 15-324, PROTEIN SEQUENCE OF 24-53.
    Strain: cv. Havana.
  4. "A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole."
    Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T.
    Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins."
    Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr.
    Science 257:655-657(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION AT PRO-67 AND PRO-69, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCHI2_TOBAC
AccessioniPrimary (citable) accession number: P24091
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: October 14, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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.