GUN_ECOLI
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 03-AUG-2022, entry version 154.
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; Proteobacteria; 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}.
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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; P37651; -.
DR PRIDE; P37651; -.
DR EnsemblBacteria; AAC76556; AAC76556; b3531.
DR EnsemblBacteria; BAE77763; BAE77763; BAE77763.
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 PhylomeDB; P37651; -.
DR BioCyc; EcoCyc:EG12258-MON; -.
DR BioCyc; MetaCyc:EG12258-MON; -.
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; SSF48208; 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
