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P06215

- CHIT_PHAVU

UniProt

P06215 - CHIT_PHAVU

Protein

Endochitinase

Gene
N/A
Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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

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

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. chitin catabolic process Source: UniProtKB-KW
    3. defense response Source: UniProtKB-KW
    4. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, 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 (EC:3.2.1.14)
    OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
    Taxonomic identifieri3885 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

    Subcellular locationi

    Vacuole By similarity
    Note: Vacuolar and protoplast.By similarity

    GO - Cellular componenti

    1. vacuole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 317290EndochitinasePRO_0000005311Add
    BLAST
    Propeptidei318 – 32811Removed in mature formCuratedPRO_0000005312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 45PROSITE-ProRule annotation
    Disulfide bondi39 ↔ 51PROSITE-ProRule annotation
    Disulfide bondi44 ↔ 58PROSITE-ProRule annotation
    Disulfide bondi62 ↔ 66PROSITE-ProRule annotation
    Disulfide bondi97 ↔ 159PROSITE-ProRule annotation
    Disulfide bondi170 ↔ 178PROSITE-ProRule annotation
    Disulfide bondi277 ↔ 309PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    ProMEXiP06215.

    Expressioni

    Inductioni

    By ethylene.

    Structurei

    3D structure databases

    ProteinModelPortaliP06215.
    SMRiP06215. Positions 28-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 6841Chitin-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.

    P06215-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKNRMMMMI WSVGVVWMLL LVGGSYGEQC GRQAGGALCP GGNCCSQFGW    50
    CGSTTDYCGP GCQSQCGGPS PAPTDLSALI SRSTFDQMLK HRNDGACPAK 100
    GFYTYDAFIA AAKAYPSFGN TGDTATRKRE IAAFLGQTSH ETTGGWATAP 150
    DGPYAWGYCF VRERNPSTYC SATPQFPCAP GQQYYGRGPI QISWNYNYGQ 200
    CGRAIGVDLL NKPDLVATDS VISFKSALWF WMTAQSPKPS SHDVITSRWT 250
    PSSADVAARR LPGYGTVTNI INGGLECGRG QDSRVQDRIG FFKRYCDLLG 300
    VGYGNNLDCY SQTPFGNSLL LSDLVTSQ 328
    Length:328
    Mass (Da):35,444
    Last modified:January 1, 1988 - v1
    Checksum:i0B5A73626C776C8A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401P → L in AAA33757. (PubMed:16665863)Curated
    Sequence conflicti54 – 541T → S AA sequence 1 PublicationCurated
    Sequence conflicti56 – 561D → E AA sequence 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881M → V.
    Natural varianti168 – 1681T → A.
    Natural varianti210 – 2101L → F.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13968 mRNA. Translation: AAA33756.1.
    M19052 mRNA. Translation: AAA33757.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13968 mRNA. Translation: AAA33756.1 .
    M19052 mRNA. Translation: AAA33757.1 .

    3D structure databases

    ProteinModelPortali P06215.
    SMRi P06215. Positions 28-316.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM18. Carbohydrate-Binding Module Family 18.
    GH19. Glycoside Hydrolase Family 19.

    Proteomic databases

    ProMEXi P06215.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.30.60.10. 1 hit.
    InterProi IPR001002. Chitin-bd_1.
    IPR018371. Chitin-binding_1_CS.
    IPR016283. Glyco_hydro_19.
    IPR000726. Glyco_hydro_19_cat.
    IPR023346. Lysozyme-like_dom.
    [Graphical view ]
    Pfami PF00187. Chitin_bind_1. 1 hit.
    PF00182. Glyco_hydro_19. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001060. Endochitinase. 1 hit.
    PRINTSi PR00451. CHITINBINDNG.
    ProDomi PD000609. Chitin_bd_1. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00270. ChtBD1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    SSF57016. SSF57016. 1 hit.
    PROSITEi PS00026. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris."
      Broglie K.E., Gaynor J.J., Broglie R.M.
      Proc. Natl. Acad. Sci. U.S.A. 83:6820-6824(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Saxa.
    2. "Amino-terminal sequence of ethylene-induced bean leaf chitinase reveals similarities to sugar-binding domains of wheat germ agglutinin."
      Lucas J., Henschen A., Lottspeich F., Voegeli U., Boller T.
      FEBS Lett. 193:208-210(1985)
      Cited for: PROTEIN SEQUENCE OF 28-57.
    3. "Chitinase cDNA cloning and mRNA induction by fungal elicitor, wounding, and infection."
      Hedrick S.A., Bell J.N., Boller T., Lamb C.J.
      Plant Physiol. 86:182-186(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-51.

    Entry informationi

    Entry nameiCHIT_PHAVU
    AccessioniPrimary (citable) accession number: P06215
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 109 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

    External Data

    Dasty 3