ID   GUNB_CELJU              Reviewed;         511 AA.
AC   P18126; B3PI35;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Endoglucanase B;
DE            Short=EGB;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=celB; Synonyms=cel45A; OrderedLocusNames=CJA_0374;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-48.
RX   PubMed=2117693; DOI=10.1111/j.1365-2958.1990.tb00646.x;
RA   Gilbert H.J., Hall J., Hazlewood G.P., Ferreira L.M.A.;
RT   "The N-terminal region of an endoglucanase from Pseudomonas fluorescens
RT   subspecies cellulosa constitutes a cellulose-binding domain that is
RT   distinct from the catalytic centre.";
RL   Mol. Microbiol. 4:759-767(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
CC   -!- FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta-
CC       glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
CC       EGB is most active against barley beta-glucan, but showed significant
CC       activity against amorphous and crystalline cellulose.
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   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC       {ECO:0000305}.
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DR   EMBL; X52615; CAA36844.1; -; Genomic_DNA.
DR   EMBL; CP000934; ACE82688.1; -; Genomic_DNA.
DR   PIR; S10527; S10527.
DR   AlphaFoldDB; P18126; -.
DR   SMR; P18126; -.
DR   STRING; 498211.CJA_0374; -.
DR   CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH45; Glycoside Hydrolase Family 45.
DR   KEGG; cja:CJA_0374; -.
DR   eggNOG; COG2730; Bacteria.
DR   HOGENOM; CLU_532865_0_0_6; -.
DR   OrthoDB; 5696284at2; -.
DR   Proteomes; UP000001036; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.30.32.30; CBM10; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR036601; CBM10_sf.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR009031; CBM_fam10.
DR   InterPro; IPR000334; Glyco_hydro_45.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR39730; ENDOGLUCANASE 1; 1.
DR   PANTHER; PTHR39730:SF1; ENDOGLUCANASE 1; 1.
DR   Pfam; PF02013; CBM_10; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02015; Glyco_hydro_45; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM01064; CBM_10; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF57615; Type X cellulose binding domain, CBDX; 1.
DR   PROSITE; PS51763; CBM10; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Periplasm;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:2117693"
FT   CHAIN           30..511
FT                   /note="Endoglucanase B"
FT                   /id="PRO_0000008023"
FT   DOMAIN          30..130
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   DOMAIN          180..209
FT                   /note="CBM10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   REGION          137..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        276
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10069"
FT   ACT_SITE        393
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        181..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        191..206
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  52078 MW;  3C3119D998291D8E CRC64;
     MNLLSGWVRP LMLGCGLLGA ALSAGSIQAA VCEYRVTNEW GSGFTASIRI TNNGSSTING
     WSVSWNYTDG SRVTSSWNAG LSGANPYSAT PVGWNTSIPI GSSVEFGVQG NNGSSRAQVP
     AVTGAICGGQ GSSAPSSVAS SSSSSSVVSS TPRSSSSSVS SSVPGTSSSS SSSVLTGAQA
     CNWYGTLTPL CNNTSNGWGY EDGRSCVART TCSAQPAPYG IVSTSSSTPL SSSSSSRSSV
     ASSSSLSSAT SSSASSVSSV PPIDGGCNGY ATRYWDCCKP HCGWSANVPS LVSPLQSCSA
     NNTRLSDVSV GSSCDGGGGY MCWDKIPFAV SPTLAYGYAA TSSGDVCGRC YQLQFTGSSY
     NAPGDPGSAA LAGKTMIVQA TNIGYDVSGG QFDILVPGGG VGAFNACSAQ WGVSNAELGA
     QYGGFLAACK QQLGYNASLS QYKSCVLNRC DSVFGSRGLT QLQQGCTWFA EWFEAADNPS
     LKYKEVPCPA ELTTRSGMNR SILNDIRNTC P
//