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Database: UniProt
Entry: Q9RI72
LinkDB: Q9RI72
Original site: Q9RI72 
ID   XYNC_STRCO              Reviewed;         241 AA.
AC   Q9RI72;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 107.
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; OrderedLocusNames=SCO0105; ORFNames=SCJ11.34c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
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 {ECO:0000250}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; AL939104; CAB52919.1; -; Genomic_DNA.
DR   PIR; T37005; T37005.
DR   RefSeq; NP_624448.1; NC_003888.3.
DR   RefSeq; WP_003978772.1; NC_003888.3.
DR   ProteinModelPortal; Q9RI72; -.
DR   SMR; Q9RI72; -.
DR   STRING; 100226.SCO0105; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   EnsemblBacteria; CAB52919; CAB52919; CAB52919.
DR   GeneID; 1095530; -.
DR   KEGG; sco:SCO0105; -.
DR   PATRIC; fig|100226.15.peg.87; -.
DR   eggNOG; ENOG4107T94; Bacteria.
DR   eggNOG; ENOG410YH6C; LUCA.
DR   HOGENOM; HOG000179135; -.
DR   InParanoid; Q9RI72; -.
DR   KO; K01181; -.
DR   OMA; IEYYVVD; -.
DR   PhylomeDB; Q9RI72; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IBA:GO_Central.
DR   GO; GO:0045493; P:xylan catabolic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     49       Tat-type signal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00648}.
FT   CHAIN        50    241       Endo-1,4-beta-xylanase C.
FT                                /FTId=PRO_0000295647.
FT   DOMAIN       51    240       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    135    135       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    227    227       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
SQ   SEQUENCE   241 AA;  25845 MW;  37B6E99DE517B78F CRC64;
     MQQDGTQQDR IKQSPAPLNG MSRRGFLGGA GTLALATASG LLLPGTAHAA TTITTNQTGT
     DGMYYSFWTD GGGSVSMTLN GGGSYSTQWT NCGNFVAGKG WSTGGRRTVR YNGYFNPSGN
     GYGCLYGWTS NPLVEYYIVD NWGSYRPTGT YKGTVSSDGG TYDIYQTTRY NAPSVEGTKT
     FQQYWSVRQS KVTSGSGTIT TGNHFDAWAR AGMNMGQFRY YMIMATEGYQ SSGSSNITVS
     G
//
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