ID   GUN_ECO57               Reviewed;         368 AA.
AC   Q8X5L9;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=Z4946, ECs4411;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG58673.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37834.1; -; Genomic_DNA.
DR   PIR; C91180; C91180.
DR   PIR; E86026; E86026.
DR   RefSeq; NP_312438.1; NC_002695.1.
DR   RefSeq; WP_001302749.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X5L9; -.
DR   SMR; Q8X5L9; -.
DR   STRING; 155864.EDL933_4786; -.
DR   CAZy; GH8; Glycoside Hydrolase Family 8.
DR   EnsemblBacteria; AAG58673; AAG58673; Z4946.
DR   EnsemblBacteria; BAB37834; BAB37834; ECs_4411.
DR   GeneID; 915724; -.
DR   KEGG; ece:Z4946; -.
DR   KEGG; ecs:ECs_4411; -.
DR   PATRIC; fig|386585.9.peg.4612; -.
DR   eggNOG; COG3405; Bacteria.
DR   HOGENOM; CLU_037297_0_0_6; -.
DR   OMA; IRVYLWV; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   InterPro; IPR019834; Glyco_hydro_8_CS.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   PRINTS; PR00735; GLHYDRLASE8.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..368
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000007939"
FT   ACT_SITE        55
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10058"
SQ   SEQUENCE   368 AA;  41760 MW;  ECFD4234AD5113D2 CRC64;
     MNVLRSGLVT MLLLAAFSVQ AACTWPAWEQ FKKDYISQEG RVIDPSDARK ITTSEGQSYG
     MFFALAANDR AAFDNILDWT QNNLAQGSLK ERLPAWLWGK KENSKWEVLD SNSASDGDVW
     MAWSLLEAGR LWKEQRYTDI GSALLKRIAR EEVVTVPGLG SMLLPGKVGF AEDNSWRFNP
     SYLPPTLAQY FTRFGAPWTT LRETNQRLLL ETAPKGFSPD WVRYEKDKGW QLKAEKTLIS
     SYDAIRVYMW VGMMPDSDPQ KARMLNRFKP MATFTEKNGY PPEKVDVATG KAQGKGPVGF
     SAAMLPFLQN RDAQAVQRQR VADNFPGSDA YYNYVLTLFG QGWDQHRFRF STKGELLPDW
     GQECANSH