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Database: UniProt
Entry: P26515
LinkDB: P26515
Original site: P26515 
ID   XYNB_STRLI              Reviewed;         335 AA.
AC   P26515;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 3.
DT   28-JUN-2023, entry version 116.
DE   RecName: Full=Endo-1,4-beta-xylanase B;
DE            Short=Xylanase B;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE   Flags: Precursor;
GN   Name=xlnB;
OS   Streptomyces lividans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 42-72.
RC   STRAIN=66 / 1326;
RX   PubMed=1743521; DOI=10.1016/0378-1119(91)90299-q;
RA   Shareck F., Roy C., Yaguchi M., Morosoli R., Kluepfel D.;
RT   "Sequences of three genes specifying xylanases in Streptomyces lividans.";
RL   Gene 107:75-82(1991).
RN   [2]
RP   SEQUENCE REVISION TO 29-32 AND 252-307.
RC   STRAIN=66 / 1326;
RX   PubMed=7533741; DOI=10.1016/0378-1119(94)00763-i;
RA   Shareck F., Biely P., Morosoli R., Kluepfel D.;
RT   "Analysis of DNA flanking the xlnB locus of Streptomyces lividans reveals
RT   genes encoding acetyl xylan esterase and the RNA component of ribonuclease
RT   P.";
RL   Gene 153:105-109(1995).
RN   [3]
RP   SEQUENCE REVISION TO 225.
RA   Shareck F.;
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Contributes to hydrolyze hemicellulose, the major component
CC       of plant cell-walls. XLNA and XLNB seem to act sequentially on the
CC       substrate to yield xylobiose and xylose as carbon sources.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; M64552; AAC06114.2; -; Genomic_DNA.
DR   PIR; JS0590; JS0590.
DR   PDB; 5EJ3; X-ray; 1.31 A; A/B=1-234.
DR   PDBsum; 5EJ3; -.
DR   AlphaFoldDB; P26515; -.
DR   SMR; P26515; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11B_STRLI; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000269|PubMed:1743521"
FT   CHAIN           42..335
FT                   /note="Endo-1,4-beta-xylanase B"
FT                   /id="PRO_0000008010"
FT   DOMAIN          44..230
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   DOMAIN          243..335
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   REGION          225..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..249
FT                   /note="Linker ('hinge') (Gly-rich box)"
FT   ACT_SITE        128
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   STRAND          47..53
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          56..64
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          77..84
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          86..96
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          101..123
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          127..137
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          143..150
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          153..165
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          170..183
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          187..191
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   HELIX           192..201
FT                   /evidence="ECO:0007829|PDB:5EJ3"
FT   STRAND          213..231
FT                   /evidence="ECO:0007829|PDB:5EJ3"
SQ   SEQUENCE   335 AA;  35575 MW;  513B1458BF8FF0CF CRC64;
     MNLLVQPRRR RRGPVTLLVR SAWAVALAAL AALMLPGTAQ ADTVVTTNQE GTNNGYYYSF
     WTDSQGTVSM NMGSGGQYST SWRNTGNFVA GKGWANGGRR TVQYSGSFNP SGNAYLALYG
     WTSNPLVEYY IVDNWGTYRP TGEYKGTVTS DGGTYDIYKT TRVNKPSVEG TRTFDQYWSV
     RQSKRTGGTI TTGNHFDAWA RAGMPLGNFS YYMIMATEGY QSSGSSSINV GGTGGGDSGG
     GDNGGGGGGC TATVSAGQKW GDRYNLDVSV SGASDWTVTM NVPSPAKVLS NWNVNASYPS
     AQTLTARLNG SGNNWGATIQ ANANWTWPSV SCSAG
//
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