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Database: UniProt
Entry: P26220
LinkDB: P26220
Original site: P26220 
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   05-DEC-2018, entry version 97.
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
RT   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
RT   exclusively mediated by the Tat protein export system.";
RL   Biochim. Biophys. Acta 1699:155-162(2004).
CC   -!- FUNCTION: Contributes to hydrolyze hemicellulose, the major
CC       component of plant cell-walls.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; 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
CC       peptide cleavage has been experimentally proven.
CC   -!- MISCELLANEOUS: Replacement of the wild-type signal peptide with a
CC       Sec-dependent signal peptide resulted in a mature product that was
CC       translocated but that lacked enzymatic activity. The lack of
CC       activity was probably due to an incorrect folding. No xylanase
CC       activity and no XlnC protein were detected in the supernatant of a
CC       tatC mutant.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; M64553; AAA26836.1; -; Genomic_DNA.
DR   PIR; JS0591; JS0591.
DR   ProteinModelPortal; P26220; -.
DR   SMR; P26220; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; 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;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     49       Tat-type signal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00648,
FT                                ECO:0000269|PubMed:1743521}.
FT   CHAIN        50    240       Endo-1,4-beta-xylanase C.
FT                                /FTId=PRO_0000008011.
FT   DOMAIN       51    239       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    134    134       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    226    226       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   MUTAGEN      23     23       R->K: 4-fold reduction of XlnC production
FT                                and severe impairment of precursor
FT                                processing. 7-fold reduction of XlnC
FT                                production and severe impairment of
FT                                precursor processing; when associated
FT                                with K-24. {ECO:0000269|PubMed:15158723}.
FT   MUTAGEN      24     24       R->K: 7-fold reduction of XlnC production
FT                                and severe impairment of precursor
FT                                processing; when associated with K-23.
FT                                {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
//
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