ID GUN2_BACSU Reviewed; 499 AA. AC P10475; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 27-MAR-2024, entry version 167. DE RecName: Full=Endoglucanase; DE EC=3.2.1.4; DE AltName: Full=Carboxymethyl-cellulase; DE Short=CMCase; DE Short=Cellulase; DE AltName: Full=Endo-1,4-beta-glucanase; DE Flags: Precursor; GN Name=eglS; Synonyms=bglC, gld; OrderedLocusNames=BSU18130; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PAP115; RX PubMed=3024130; DOI=10.1093/nar/14.22.9159; RA Mackay R.M., Lo A., Willick G., Zuker M., Baird S., Dove M., Moranelli F., RA Seligy V.; RT "Structure of a Bacillus subtilis endo-beta-1,4-glucanase gene."; RL Nucleic Acids Res. 14:9159-9170(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CK-2; RX PubMed=7710280; DOI=10.1007/bf00882768; RA Lindahl V., Aa K., Tronsmo A.; RT "Nucleotide sequence of an endo-beta-1,4-glucanase gene from Bacillus RT subtilis CK-2."; RL Antonie Van Leeuwenhoek 66:327-332(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=8969507; DOI=10.1099/13500872-142-11-3097; RA Rose M., Entian K.-D.; RT "New genes in the 170 degrees region of the Bacillus subtilis genome encode RT DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid RT transporter."; RL Microbiology 142:3097-3101(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [5] RP PROTEIN SEQUENCE OF 30-45. RC STRAIN=CK-2; RX PubMed=7710279; DOI=10.1007/bf00882767; RA Aa K., Flengsrud R., Lindahl V., Tronsmo A.; RT "Characterization of production and enzyme properties of an endo-beta-1,4- RT glucanase from Bacillus subtilis CK-2 isolated from compost soil."; RL Antonie Van Leeuwenhoek 66:319-326(1994). 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA97610.1; Type=Erroneous initiation; Evidence={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; Z29076; CAA82317.1; -; Genomic_DNA. DR EMBL; X04689; CAA28392.1; -; Genomic_DNA. DR EMBL; X67044; CAA47429.1; -; Genomic_DNA. DR EMBL; Z73234; CAA97610.1; ALT_INIT; Genomic_DNA. DR EMBL; AL009126; CAB13696.2; -; Genomic_DNA. DR PIR; G69593; G69593. DR RefSeq; NP_389695.2; NC_000964.3. DR RefSeq; WP_003231540.1; NZ_JNCM01000035.1. DR PDB; 2L8A; NMR; -; A=354-499. DR PDB; 3PZT; X-ray; 1.97 A; A/B=27-332. DR PDB; 3PZU; X-ray; 2.10 A; A/B=27-332. DR PDB; 3PZV; X-ray; 2.87 A; A/B/C/D=27-332. DR PDB; 6UFV; X-ray; 1.06 A; A=354-499. DR PDB; 6UFW; X-ray; 1.28 A; A=354-499. DR PDBsum; 2L8A; -. DR PDBsum; 3PZT; -. DR PDBsum; 3PZU; -. DR PDBsum; 3PZV; -. DR PDBsum; 6UFV; -. DR PDBsum; 6UFW; -. DR AlphaFoldDB; P10475; -. DR BMRB; P10475; -. DR SMR; P10475; -. DR STRING; 224308.BSU18130; -. DR CAZy; CBM3; Carbohydrate-Binding Module Family 3. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR PaxDb; 224308-BSU18130; -. DR EnsemblBacteria; CAB13696; CAB13696; BSU_18130. DR GeneID; 938607; -. DR KEGG; bsu:BSU18130; -. DR PATRIC; fig|224308.179.peg.1977; -. DR eggNOG; COG2730; Bacteria. DR InParanoid; P10475; -. DR OrthoDB; 154460at2; -. DR BioCyc; BSUB:BSU18130-MONOMER; -. DR BRENDA; 3.2.1.4; 658. DR EvolutionaryTrace; P10475; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030248; F:cellulose binding; IEA:InterPro. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central. DR Gene3D; 2.60.40.710; Endoglucanase-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR001956; CBM3. DR InterPro; IPR036966; CBM3_sf. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR018087; Glyco_hydro_5_CS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1. DR Pfam; PF00942; CBM_3; 1. DR Pfam; PF00150; Cellulase; 1. DR SMART; SM01067; CBM_3; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1. DR PROSITE; PS51172; CBM3; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Direct protein sequencing; Glycosidase; Hydrolase; KW Polysaccharide degradation; Reference proteome; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000269|PubMed:7710279" FT CHAIN 30..499 FT /note="Endoglucanase" FT /id="PRO_0000007840" FT DOMAIN 350..499 FT /note="CBM3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513" FT ACT_SITE 169 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O85465" FT ACT_SITE 257 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 65 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 69..70 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 96 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 131 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 231 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 263..264 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 291 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 296..298 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT CONFLICT 283 FT /note="S -> N (in Ref. 2; CAA47429)" FT /evidence="ECO:0000305" FT HELIX 36..39 FT /evidence="ECO:0007829|PDB:3PZU" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 76..85 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 89..98 FT /evidence="ECO:0007829|PDB:3PZT" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 109..122 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:3PZT" FT TURN 138..141 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 142..156 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:3PZT" FT TURN 176..179 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 180..194 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 211..215 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 224..231 FT /evidence="ECO:0007829|PDB:3PZT" FT TURN 232..234 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 237..248 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 253..261 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 271..283 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:3PZT" FT HELIX 320..330 FT /evidence="ECO:0007829|PDB:3PZT" FT STRAND 354..360 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 372..378 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 380..382 FT /evidence="ECO:0007829|PDB:6UFV" FT HELIX 386..388 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 389..395 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 402..409 FT /evidence="ECO:0007829|PDB:6UFV" FT HELIX 413..415 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 416..427 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 430..440 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 447..450 FT /evidence="ECO:0007829|PDB:2L8A" FT STRAND 452..458 FT /evidence="ECO:0007829|PDB:6UFV" FT HELIX 466..468 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 482..488 FT /evidence="ECO:0007829|PDB:6UFV" FT STRAND 491..495 FT /evidence="ECO:0007829|PDB:6UFV" SQ SEQUENCE 499 AA; 55287 MW; 8F735FF711B3EAE2 CRC64; MKRSISIFIT CLLITLLTMG GMIASPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK GISSHGLQWY GEYVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQFLR DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLKY LDSKTISWVN WNLSDKQESS SALKPGASKT GGWRLSDLSA SGTFVRENIL GTKDSTKDIP ETPSKDKPTQ ENGISVQYRA GDGSMNSNQI RPQLQIKNNG NTTVDLKDVT ARYWYKAKNK GQNFDCDYAQ IGCGNVTHKF VTLHKPKQGA DTYLELGFKN GTLAPGASTG NIQLRLHNDD WSNYAQSGDY SFFKSNTFKT TKKITLYDQG KLIWGTEPN //