ID   GUN_XANAC               Reviewed;         384 AA.
AC   P58935;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethylcellulase;
DE            Short=CMCase;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=bcsZ; OrderedLocusNames=XAC3516;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Hydrolyzes carboxymethylcellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC       {ECO:0000305}.
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DR   EMBL; AE008923; AAM38359.1; -; Genomic_DNA.
DR   AlphaFoldDB; P58935; -.
DR   SMR; P58935; -.
DR   STRING; 190486.XAC3516; -.
DR   CAZy; GH8; Glycoside Hydrolase Family 8.
DR   EnsemblBacteria; AAM38359; AAM38359; XAC3516.
DR   KEGG; xac:XAC3516; -.
DR   eggNOG; COG3405; Bacteria.
DR   HOGENOM; CLU_037297_0_0_6; -.
DR   OMA; IRVYLWV; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000000576; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR002037; Glyco_hydro_8.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   PRINTS; PR00735; GLHYDRLASE8.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..384
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000007943"
FT   ACT_SITE        63
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        124
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   384 AA;  41510 MW;  4DD7FB6CF822D127 CRC64;
     MTRRRLLHAG TLAGVAALLP AAALAAPSQC GPWPLWSAFV DKHIQRDGRV VDFLNPDQRS
     TSEGQSYALF FALVNNDQVL FDKVLSWTRH NLCGGRPDLN LPAWLWGRDG SGAWRVLDAN
     TASDGELWIA YALLEAGRLW SRPGFLKAGQ QMLQLIRTQE VATLPGLGPM LLPGRTGFVD
     NGRWTLNPSY LPIQVLRRCA NADPKGPWAA IAANSARVLR DSAPVGFAPD WTVWDGKTFN
     ADPKRGNVGS YDAIRVYLWA GMLDAGEPLR ARLLQDLSGP ADLLAAQQTP AEKIDTARGV
     GTGALPVGFS AALLPYLSAL GKPALLKAQA QRVPAATQPA AAALPYFERT LALFGQGWLE
     NRYRFAADGR LLPAWRTPAC AATT