ID   GUNA_PAELA              Reviewed;         700 AA.
AC   P29719;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Endoglucanase A;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase A;
DE   AltName: Full=EG-A;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=celA;
OS   Paenibacillus lautus (Bacillus lautus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1401;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PL236;
RX   PubMed=1592807; DOI=10.1128/jb.174.11.3522-3531.1992;
RA   Hansen C.K., Diderichsen B., Joergensen P.L.;
RT   "celA from Bacillus lautus PL236 encodes a novel cellulose-binding endo-
RT   beta-1,4-glucanase.";
RL   J. Bacteriol. 174:3522-3531(1992).
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   -!- PTM: A short form (EG-A-S) arises from post-translational proteolysis
CC       of approximately 150 AA at the C-terminus of EG-A-L.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 44 (cellulase J) family.
CC       {ECO:0000305}.
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DR   EMBL; M76588; AAA22303.1; -; Genomic_DNA.
DR   PIR; B41897; B41897.
DR   AlphaFoldDB; P29719; -.
DR   SMR; P29719; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH44; Glycoside Hydrolase Family 44.
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; 2.60.40.1180; -; 1.
DR   Gene3D; 2.60.40.710; -; 1.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR024745; Glyco_hydro_44.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF12891; Glyco_hydro_44; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51172; CBM3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..700
FT                   /note="Endoglucanase A"
FT                   /id="PRO_0000008021"
FT   DOMAIN          550..700
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   ACT_SITE        213
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   700 AA;  76910 MW;  3D5C8CADA53EEE0F CRC64;
     MKTRQRKRLF VSAALAVSLT MTVPMPASVN AAASDVTFTI NTQSERAAIS PNIYGTNQDL
     SGTENWSSRR LGGNRLTGYN WENNASSAGR DWLHYSDDFL CGNGGVPDTD CDKPGAVVTA
     FHDKSLENGA YSIVTLQMAG YVSRDKNGPV DESETAPSPR WDKVEFAKNA PFSLQPHLND
     GQVYMDEEVN FLVNRYGNAS TSTGIKAYSL DNEPALWSET HPRIHPEQLQ AAELVAKSID
     LSKAVKNVDP HAEIFGPALY GFGAYLSLQD APGWPSLQGN YSWFIDYYLD QMKNAHTQNG
     KRLLDVLDVH WYPEAQGGGQ RIVFGGAGNI DTQKARVQAP RSLWDPAYQE DSWIGTWFSS
     YLPLIPKLQS SIQTYYPGTK LAITESSYGG DNHISGGIAT ADALGIFGKY GVYAANYWQT
     EDNTDYTSAA YKLYRNYDGN KSGFGSIKVD AATSDTENSS VYASVTDEEN SELHLIVLNK
     NFDDPINATF QLSGDKTYTS GRVWGFDQTG SDITEQAAIT NINNNQFTYT LPPLSAYHIV
     LKADSTEPVN SDLVVQYKDG DRNNATDNQI KPHFNIQNKG TSPVDLSSLT LRYYFTKDSS
     AAMNGWIDWA KLGGSNIQIS FGNHNGADSD TYAELGFSSG AGSIAEGGQS GEIQLRMSKA
     DWSNFNEAND YSFDGAKTAY IDWDRVTLYQ DGQLVWGIEP