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P26220

- XYNC_STRLI

UniProt

P26220 - XYNC_STRLI

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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

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 – 1341Nucleophile By similarity
Active sitei226 – 2261Proton donor By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

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
Complete GO annotation...

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 PublicationAdd
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.

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: November 13, 2013
This is version 83 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

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