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Database: UniProt
Entry: Q93TJ6_BACIU
LinkDB: Q93TJ6_BACIU
Original site: Q93TJ6_BACIU 
ID   Q93TJ6_BACIU            Unreviewed;       499 AA.
AC   Q93TJ6;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN   Name=cel {ECO:0000313|EMBL:AAK39540.1};
GN   Synonyms=celW {ECO:0000313|EMBL:AHZ62779.1}, eglS
GN   {ECO:0000313|EMBL:ADP05286.1};
OS   Bacillus subtilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423 {ECO:0000313|EMBL:AAK39540.1};
RN   [1] {ECO:0000313|EMBL:AAK39540.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Y106 {ECO:0000313|EMBL:AAK39540.1};
RA   Qi M., Wang P., Liu X., Qu Y.;
RT   "The cloning and expression of a cellulase from Bacillus subtilis Y106.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADP05286.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Shu-3 {ECO:0000313|EMBL:ADP05286.1};
RA   Zhang Y.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ADM12805.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BEC-1 {ECO:0000313|EMBL:ADM12805.1};
RA   Zhu C., Xu Z., Song R.;
RT   "The endoglucanase from Bacillus subtilis BEC-1 bears halo-tolerant,
RT   acidophilic and dithiothreitol-stimulated enzyme activity.";
RL   World J. Microbiol. Biotechnol. 27:2863-2871(2011).
RN   [4] {ECO:0000313|EMBL:AIV00153.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ho27 {ECO:0000313|EMBL:AIV00153.1};
RA   Ibrahim A.M., Ismael H.M., Helal G.E.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:AHZ62779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WL001 {ECO:0000313|EMBL:AHZ62779.1};
RA   Wang L., Chen Y.;
RT   "Coexpression and secretion of endoglucanase and phytase genes in
RT   Lactobacillus reuteri.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000966,
CC         ECO:0000256|RuleBase:RU361153};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR   EMBL; AF355629; AAK39540.1; -; Genomic_DNA.
DR   EMBL; HQ000093; ADM12805.1; -; Genomic_DNA.
DR   EMBL; HM470252; ADP05286.1; -; Genomic_DNA.
DR   EMBL; KJ528404; AHZ62779.1; -; Genomic_DNA.
DR   EMBL; KF792058; AIV00153.1; -; Genomic_DNA.
DR   RefSeq; WP_046381055.1; NZ_NJRC01000007.1.
DR   AlphaFoldDB; Q93TJ6; -.
DR   SMR; Q93TJ6; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
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; 2.60.40.710; 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   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361153};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:ADP05286.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361153}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..499
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007715582"
FT   DOMAIN          350..499
FT                   /note="CBM3"
FT                   /evidence="ECO:0000259|PROSITE:PS51172"
SQ   SEQUENCE   499 AA;  55252 MW;  587A687584B7E5BE CRC64;
     MKRSISIFIT CLLITLLTMG GMLASPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK
     GISSHGLQWY GEYVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK
     ELGIYVIIDW HILNDGNPNH NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI
     KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQFLR
     DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLKY LDSKTISWVN WNLSDKQESS
     SALKPGASKT GGWQLSDLSA SGTFVRENIL GTKDSTKDIP ETPAKDKPTQ ENGISVQYRA
     GDGSMNSNQI RPQLQIKNNG NTTVDLKDVT ARYWYKAKNK GQNFDCDYAQ IGCGNVTHKF
     VTLHKPKQGA DTYLELGFKN GTLAPGASTG NIQLRLHNDD WSNYAQSGDY SFFKSNTFKT
     TKKITLYDQG KLIWGTEPN
//
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