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Protein

Endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Streptomyces lividans
Status
Reviewed-Annotation score: 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 – 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
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 signalPROSITE-ProRule annotation1 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
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

        10         20         30         40         50
MQQDGTQQDR IKQSPAPLNG MSRRGFLGGA GTLALATASG LLLPGTAHAA
60 70 80 90 100
TTITTNQTGT DGMYYSFWTD GGGSVSMTLN GGGSYSTQWT NCGNFVAGKG
110 120 130 140 150
WSTGDGNVRY NGYFNPVGNG YGCLYGWTSN PLVEYYIVDN WGSYRPTGTY
160 170 180 190 200
KGTVSSDGGT YDIYQTTRYN APSVEGTKTF QQYWSVRQSK VTSGSGTITT
210 220 230 240
GNHFDAWARA GMNMGQFRYY MIMATEGYQS SGSSNITVSG
Length:240
Mass (Da):25,673
Last modified:April 30, 1992 - v1
Checksum:iFC663415780142CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64553 Genomic DNA. Translation: AAA26836.1.
PIRiJS0591.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64553 Genomic DNA. Translation: AAA26836.1.
PIRiJS0591.

3D structure databases

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

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
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]
ProtoNetiSearch...

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(1990) [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(2003) [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: April 30, 1992
Last sequence update: April 30, 1992
Last modified: January 6, 2015
This is version 86 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

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 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.