P26220 (XYNC_STRLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Streptomyces lividans

Taxonomic identifier

1916 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 49	49	Tat-type signal Ref.1
	Chain	50 – 240	191	Endo-1,4-beta-xylanase C		PRO_0000008011
Sites
	Active site	134	1	Nucleophile By similarity
	Active site	226	1	Proton donor By similarity
Experimental info
	Mutagenesis	23	1	R → 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
	Mutagenesis	24	1	R → K: 7-fold reduction of XlnC production and severe impairment of precursor processing; when associated with K-23. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P26220 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: FC663415780142CA	FASTA	240	25,673
	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

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.
PIR	JS0591.
3D structure databases
ProteinModelPortal	P26220.
SMR	P26220. Positions 53-236.
ModBase	Search...
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
Gene3D	2.60.120.180. 1 hit.
InterPro	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]
Pfam	PF00457. Glyco_hydro_11. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
TIGRFAMs	TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNC_STRLI

Accession

Primary (citable) accession number: P26220

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program