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P26220 (XYNC_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase C

Short name=Xylanase C
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
Gene names
Name:xlnC
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted.

Post-translational modification

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

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.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4949Tat-type signal Ref.1
Chain50 – 240191Endo-1,4-beta-xylanase C
PRO_0000008011

Sites

Active site1341Nucleophile By similarity
Active site2261Proton donor By similarity

Experimental info

Mutagenesis231R → 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. Ref.2
Mutagenesis241R → K: 7-fold reduction of XlnC production and severe impairment of precursor processing; when associated with K-23. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P26220 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: FC663415780142CA

FASTA24025,673
        10         20         30         40         50         60 
MQQDGTQQDR IKQSPAPLNG MSRRGFLGGA GTLALATASG LLLPGTAHAA TTITTNQTGT 

        70         80         90        100        110        120 
DGMYYSFWTD GGGSVSMTLN GGGSYSTQWT NCGNFVAGKG WSTGDGNVRY NGYFNPVGNG 

       130        140        150        160        170        180 
YGCLYGWTSN PLVEYYIVDN WGSYRPTGTY KGTVSSDGGT YDIYQTTRYN APSVEGTKTF 

       190        200        210        220        230        240 
QQYWSVRQSK VTSGSGTITT GNHFDAWARA GMNMGQFRYY MIMATEGYQS SGSSNITVSG 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64553 Genomic DNA. Translation: AAA26836.1.
PIRJS0591.

3D structure databases

ProteinModelPortalP26220.
SMRP26220. Positions 53-236.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. 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]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. SSF49899. 1 hit.
TIGRFAMsTIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNC_STRLI
AccessionPrimary (citable) accession number: P26220
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries