ID   XYNC_STRLI              Reviewed;         240 AA.
AC   P26220;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Endo-1,4-beta-xylanase C;
DE            Short=Xylanase C;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase C;
DE   Flags: Precursor;
GN   Name=xlnC;
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 50-80.
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   EXPORT VIA THE TAT-SYSTEM, AND MUTAGENESIS OF ARG-23 AND ARG-24.
RX   PubMed=15158723; DOI=10.1016/j.bbapap.2004.02.008;
RA   Faury D., Saidane S., Li H., Morosoli R.;
RT   "Secretion of active xylanase C from Streptomyces lividans is exclusively
RT   mediated by the Tat protein export system.";
RL   Biochim. Biophys. Acta 1699:155-162(2004).
CC   -!- FUNCTION: Contributes to hydrolyze hemicellulose, the major component
CC       of plant cell-walls.
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   -!- PTM: Exported by the Tat system. The position of the signal peptide
CC       cleavage has been experimentally proven.
CC   -!- MISCELLANEOUS: Replacement of the wild-type signal peptide with a Sec-
CC       dependent signal peptide resulted in a mature product that was
CC       translocated but that lacked enzymatic activity. The lack of activity
CC       was probably due to an incorrect folding. No xylanase activity and no
CC       XlnC protein were detected in the supernatant of a tatC mutant.
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; M64553; AAA26836.1; -; Genomic_DNA.
DR   PIR; JS0591; JS0591.
DR   AlphaFoldDB; P26220; -.
DR   SMR; P26220; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11C_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:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
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   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..49
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:1743521"
FT   CHAIN           50..240
FT                   /note="Endo-1,4-beta-xylanase C"
FT                   /id="PRO_0000008011"
FT   DOMAIN          51..239
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        134
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        226
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   MUTAGEN         23
FT                   /note="R->K: 4-fold reduction of XlnC production and severe
FT                   impairment of precursor processing. 7-fold reduction of
FT                   XlnC production and severe impairment of precursor
FT                   processing; when associated with K-24."
FT                   /evidence="ECO:0000269|PubMed:15158723"
FT   MUTAGEN         24
FT                   /note="R->K: 7-fold reduction of XlnC production and severe
FT                   impairment of precursor processing; when associated with K-
FT                   23."
FT                   /evidence="ECO:0000269|PubMed:15158723"
SQ   SEQUENCE   240 AA;  25673 MW;  FC663415780142CA CRC64;
     MQQDGTQQDR IKQSPAPLNG MSRRGFLGGA GTLALATASG LLLPGTAHAA TTITTNQTGT
     DGMYYSFWTD GGGSVSMTLN GGGSYSTQWT NCGNFVAGKG WSTGDGNVRY NGYFNPVGNG
     YGCLYGWTSN PLVEYYIVDN WGSYRPTGTY KGTVSSDGGT YDIYQTTRYN APSVEGTKTF
     QQYWSVRQSK VTSGSGTITT GNHFDAWARA GMNMGQFRYY MIMATEGYQS SGSSNITVSG