XYNB_STRLI
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 25-MAY-2022, entry version 112.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF49899; SSF49899; 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
