P26515 (XYNB_STRLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase B
Short name=Xylanase B
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B

Gene names

Name:

xlnB

Organism

Streptomyces lividans

Taxonomic identifier

1916 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	335 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. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. Contains 1 CBM2 (carbohydrate binding type-2) domain.

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 polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 41	41	Ref.1
	Chain	42 – 335	294	Endo-1,4-beta-xylanase B		PRO_0000008010
Regions
	Domain	250 – 335	86	CBM2
	Region	42 – 230	189	Catalytic
	Region	231 – 249	19	Linker ("hinge") (Gly-rich box)
Sites
	Active site	128	1	Nucleophile By similarity
	Active site	218	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26515 [UniParc]. Last modified August 14, 2001. Version 3. Checksum: 513B1458BF8FF0CF	FASTA	335	35,575
	10 20 30 40 50 60 MNLLVQPRRR RRGPVTLLVR SAWAVALAAL AALMLPGTAQ ADTVVTTNQE GTNNGYYYSF 70 80 90 100 110 120 WTDSQGTVSM NMGSGGQYST SWRNTGNFVA GKGWANGGRR TVQYSGSFNP SGNAYLALYG 130 140 150 160 170 180 WTSNPLVEYY IVDNWGTYRP TGEYKGTVTS DGGTYDIYKT TRVNKPSVEG TRTFDQYWSV 190 200 210 220 230 240 RQSKRTGGTI TTGNHFDAWA RAGMPLGNFS YYMIMATEGY QSSGSSSINV GGTGGGDSGG 250 260 270 280 290 300 GDNGGGGGGC TATVSAGQKW GDRYNLDVSV SGASDWTVTM NVPSPAKVLS NWNVNASYPS 310 320 330 AQTLTARLNG SGNNWGATIQ ANANWTWPSV SCSAG

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 42-72. Strain: 66 / 1326.
[2]	"Analysis of DNA flanking the xlnB locus of Streptomyces lividans reveals genes encoding acetyl xylan esterase and the RNA component of ribonuclease P." Shareck F., Biely P., Morosoli R., Kluepfel D. Gene 153:105-109(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 29-32 AND 252-307. Strain: 66 / 1326.
[3]	Shareck F. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 225.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64552 Genomic DNA. Translation: AAC06114.2.
PIR	JS0590.
3D structure databases
ProteinModelPortal	P26515.
SMR	P26515. Positions 45-228.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. 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. 2.60.40.290. 1 hit.
InterPro	IPR008965. Carb-bd_dom. IPR012291. CBD_carb-bd_dom. IPR001919. Cellulose-bd_dom_fam2_bac. IPR008985. ConA-like_lec_gl_sf. IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12. IPR018208. Glyco_hydro_11_AS. [Graphical view]
Pfam	PF00457. Glyco_hydro_11. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
SMART	SM00637. CBD_II. 1 hit. [Graphical view]
SUPFAM	SSF49384. Cellul_bind. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS51173. CBM2. 1 hit. PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNB_STRLI

Accession

Primary (citable) accession number: P26515

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 14, 2001
Last modified:	April 3, 2013
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program