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 13-SEP-2023, entry version 108.
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; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; 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}.
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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 NCBIfam; TIGR01409; TAT_signal_seq; 1.
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 SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//
