GUNB_CELJU
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 25-MAY-2022, entry version 131.
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; Proteobacteria; 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 EnsemblBacteria; ACE82688; ACE82688; CJA_0374.
DR KEGG; cja:CJA_0374; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_532865_0_0_6; -.
DR OMA; PEAYNAN; -.
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; 2.30.32.30; -; 1.
DR Gene3D; 2.40.40.10; -; 1.
DR Gene3D; 2.60.40.290; -; 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 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; SSF49384; SSF49384; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR SUPFAM; SSF57615; SSF57615; 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
