ID GUN_ECOLI Reviewed; 368 AA. AC P37651; Q2M7J3; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 24-JAN-2024, entry version 160. 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; Synonyms=bcsC, yhjM; OrderedLocusNames=b3531, JW3499; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=10102357; DOI=10.1007/s004380050962; RA Park Y.W., Yun H.D.; RT "Cloning of the Escherichia coli endo-1,4-D-glucanase gene and RT identification of its product."; RL Mol. Gen. Genet. 261:236-241(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8041620; DOI=10.1093/nar/22.13.2576; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region RT from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP CHARACTERIZATION. RC STRAIN=ECOR 10, ECOR 12, and TOB1; RX PubMed=11260463; DOI=10.1046/j.1365-2958.2001.02337.x; RA Zogaj X., Nimtz M., Rohde M., Bokranz W., Roemling U.; RT "The multicellular morphotypes of Salmonella typhimurium and Escherichia RT coli produce cellulose as the second component of the extracellular RT matrix."; RL Mol. Microbiol. 39:1452-1463(2001). CC -!- FUNCTION: Hydrolyzes carboxymethylcellulose. 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. CC -!- MISCELLANEOUS: The genes bscA, bcsB, bcsZ and bcsC are constitutively CC transcribed but cellulose synthesis occurs only when DgcC, a putative CC transmembrane protein regulated by CsgD, is expressed. Cellulose CC production is abolished in E.coli K12. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00039; AAB18508.1; -; Genomic_DNA. DR EMBL; U00096; AAC76556.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77763.1; -; Genomic_DNA. DR PIR; S47752; S47752. DR RefSeq; NP_417988.1; NC_000913.3. DR RefSeq; WP_001311203.1; NZ_LN832404.1. DR PDB; 3QXF; X-ray; 1.85 A; A/B/C/D=22-368. DR PDB; 3QXQ; X-ray; 2.20 A; A/B/C/D=22-368. DR PDBsum; 3QXF; -. DR PDBsum; 3QXQ; -. DR AlphaFoldDB; P37651; -. DR SMR; P37651; -. DR BioGRID; 4263272; 100. DR IntAct; P37651; 4. DR STRING; 511145.b3531; -. DR CAZy; GH8; Glycoside Hydrolase Family 8. DR TCDB; 4.D.3.1.6; the glycan glucosyl transferase (opgh) family. DR PaxDb; 511145-b3531; -. DR EnsemblBacteria; AAC76556; AAC76556; b3531. DR GeneID; 948046; -. DR KEGG; ecj:JW3499; -. DR KEGG; eco:b3531; -. DR PATRIC; fig|511145.12.peg.3642; -. DR EchoBASE; EB2167; -. DR eggNOG; COG3405; Bacteria. DR HOGENOM; CLU_037297_0_0_6; -. DR InParanoid; P37651; -. DR OMA; IRVYLWV; -. DR OrthoDB; 9766708at2; -. DR PhylomeDB; P37651; -. DR BioCyc; EcoCyc:EG12258-MONOMER; -. DR BioCyc; MetaCyc:EG12258-MONOMER; -. DR BRENDA; 3.2.1.4; 2026. DR UniPathway; UPA00694; -. DR PRO; PR:P37651; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005576; C:extracellular region; IDA:EcoCyc. DR GO; GO:0008810; F:cellulase activity; IDA:EcoCyc. 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; Six-hairpin glycosidases; 1. DR PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..368 FT /note="Endoglucanase" FT /id="PRO_0000007938" 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" FT HELIX 26..35 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 54..66 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 70..84 FT /evidence="ECO:0007829|PDB:3QXF" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 96..100 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 115..131 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 135..152 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 153..156 FT /evidence="ECO:0007829|PDB:3QXF" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 160..163 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 165..172 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 185..191 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 198..211 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 220..225 FT /evidence="ECO:0007829|PDB:3QXF" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:3QXF" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 245..252 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 259..267 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 269..278 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:3QXF" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 298..307 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 311..323 FT /evidence="ECO:0007829|PDB:3QXF" FT HELIX 331..344 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 347..350 FT /evidence="ECO:0007829|PDB:3QXF" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:3QXF" SQ SEQUENCE 368 AA; 41700 MW; 6539C03D4D0CFDEA CRC64; MNVLRSGIVT MLLLAAFSVQ AACTWPAWEQ FKKDYISQEG RVIDPSDARK ITTSEGQSYG MFSALAANDR 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 //