Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P26220

- XYNC_STRLI

UniProt

P26220 - XYNC_STRLI

Protein

Endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Streptomyces lividans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Contributes to hydrolyze hemicellulose, the major component of plant cell-walls.

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei134 – 1341NucleophilePROSITE-ProRule annotation
    Active sitei226 – 2261Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase C (EC:3.2.1.8)
    Short name:
    Xylanase C
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase C
    Gene namesi
    Name:xlnC
    OrganismiStreptomyces lividans
    Taxonomic identifieri1916 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 231R → K: 4-fold reduction of XlnC production and severe impairment of precursor processing. 7-fold reduction of XlnC production and severe impairment of precursor processing; when associated with K-24. 1 Publication
    Mutagenesisi24 – 241R → K: 7-fold reduction of XlnC production and severe impairment of precursor processing; when associated with K-23. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4949Tat-type signal1 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Chaini50 – 240191Endo-1,4-beta-xylanase CPRO_0000008011Add
    BLAST

    Post-translational modificationi

    Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

    Structurei

    3D structure databases

    ProteinModelPortaliP26220.
    SMRiP26220. Positions 53-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    IPR006311. TAT_signal.
    IPR019546. TAT_signal_bac_arc.
    [Graphical view]
    PfamiPF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    TIGRFAMsiTIGR01409. TAT_signal_seq. 1 hit.
    PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P26220-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQQDGTQQDR IKQSPAPLNG MSRRGFLGGA GTLALATASG LLLPGTAHAA    50
    TTITTNQTGT DGMYYSFWTD GGGSVSMTLN GGGSYSTQWT NCGNFVAGKG 100
    WSTGDGNVRY NGYFNPVGNG YGCLYGWTSN PLVEYYIVDN WGSYRPTGTY 150
    KGTVSSDGGT YDIYQTTRYN APSVEGTKTF QQYWSVRQSK VTSGSGTITT 200
    GNHFDAWARA GMNMGQFRYY MIMATEGYQS SGSSNITVSG 240
    Length:240
    Mass (Da):25,673
    Last modified:May 1, 1992 - v1
    Checksum:iFC663415780142CA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64553 Genomic DNA. Translation: AAA26836.1.
    PIRiJS0591.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64553 Genomic DNA. Translation: AAA26836.1 .
    PIRi JS0591.

    3D structure databases

    ProteinModelPortali P26220.
    SMRi P26220. Positions 53-236.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Family and domain databases

    Gene3Di 2.60.120.180. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    IPR006311. TAT_signal.
    IPR019546. TAT_signal_bac_arc.
    [Graphical view ]
    Pfami PF00457. Glyco_hydro_11. 1 hit.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    TIGRFAMsi TIGR01409. TAT_signal_seq. 1 hit.
    PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequences of three genes specifying xylanases in Streptomyces lividans."
      Shareck F., Roy C., Yaguchi M., Morosoli R., Kluepfel D.
      Gene 107:75-82(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 50-80.
      Strain: 66 / 1326.
    2. "Secretion of active xylanase C from Streptomyces lividans is exclusively mediated by the Tat protein export system."
      Faury D., Saidane S., Li H., Morosoli R.
      Biochim. Biophys. Acta 1699:155-162(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: EXPORT VIA THE TAT-SYSTEM, MUTAGENESIS OF ARG-23 AND ARG-24.

    Entry informationi

    Entry nameiXYNC_STRLI
    AccessioniPrimary (citable) accession number: P26220
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Replacement of the wild-type signal peptide with a Sec-dependent signal peptide resulted in a mature product that was translocated but that lacked enzymatic activity. The lack of activity was probably due to an incorrect folding. No xylanase activity and no XlnC protein were detected in the supernatant of a tatC mutant.

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3