ID   XY11B_CELJA             Reviewed;         357 AA.
AC   Q8VP72;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Endo-1,4-beta-xylanase Xyn11B;
DE            Short=Xylanase 11B;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   Flags: Precursor;
GN   Name=xyn11B;
OS   Cellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=155077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, CATALYTIC
RP   ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=12107129; DOI=10.1128/jb.184.15.4124-4133.2002;
RA   Emami K., Nagy T., Fontes C.M., Ferreira L.M., Gilbert H.J.;
RT   "Evidence for temporal regulation of the two Pseudomonas cellulosa
RT   xylanases belonging to glycoside hydrolase family 11.";
RL   J. Bacteriol. 184:4124-4133(2002).
CC   -!- FUNCTION: Endo-acting xylanase which specifically cleaves internal
CC       linkages on the xylan backbone, releasing xylooligosaccharides. Is able
CC       to hydrolyze glucuronoxylan and the arabinoxylan from wheat.
CC       {ECO:0000269|PubMed:12107129}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000269|PubMed:12107129};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12107129}.
CC   -!- INDUCTION: Induced when the bacterium is cultured on xylan or beta-
CC       glucan but not on medium containing mannan. Is repressed by glucose.
CC       Transcription of xyn11B occurs later than transcription of xyn11A. Is
CC       expressed at maximum level in mid-log phase, and its transcription
CC       persists into the late exponential and early stationary phases.
CC       {ECO:0000269|PubMed:12107129}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; AY065640; AAL57754.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VP72; -.
DR   SMR; Q8VP72; -.
DR   CAZy; CBM60; Carbohydrate-Binding Module Family 60.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11B_CELJA; -.
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:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR031768; CBM60_xylan-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF16841; CBM60; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..357
FT                   /note="Endo-1,4-beta-xylanase Xyn11B"
FT                   /id="PRO_0000424661"
FT   DOMAIN          29..226
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   REGION          220..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  37912 MW;  42FA4BCBBB29A159 CRC64;
     MKIFQNTKNV IVSIAWAAAL CTSAVSAQTL TSNSTGTNNG FYYTFWKDSG DASMTLLSGG
     RYQSSWNSST NNWVGGKGWN PGSSSRVISY SGYYGVDSSQ NSYLALYGWT RSPLIEYYVI
     ESYGSYNPAS CSGGTDYGSF QSDGATYNVR RCQRVNQPSI DGNQTFYQYF SVRNPKKGFG
     NISGTITFAN HANFWATKGL NLGNHNYQVL ATEGYQSRGS SDITVSQGGS SGGGNSSSSS
     SASGGGSKII VVRARGTAGG ESITLRVGNT NVATWTLTTT MTNYTATTSA SGGSLVQYTN
     DSGNRDVQVD YISVNGSIRQ SEDQTYNTGV YQNGSCGGGN GRSEWLHCNG AIGYGDI