ID   GUNA_PAEBA              Reviewed;         400 AA.
AC   O08342;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-MAY-2023, entry version 76.
DE   RecName: Full=Endoglucanase A;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase A;
DE   AltName: Full=Endo-1,4-beta-D-glucanase A;
DE   Flags: Precursor;
GN   Name=celA;
OS   Paenibacillus barcinonensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=198119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, BIOTECHNOLOGY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX   PubMed=9720200; DOI=10.1007/s002530051255;
RA   Blanco A., Diaz P., Martinez J., Vidal T., Torres A.L., Pastor F.I.J.;
RT   "Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and
RT   characterisation of the enzyme. Performance in paper manufacture from
RT   cereal straw.";
RL   Appl. Microbiol. Biotechnol. 50:48-54(1998).
CC   -!- FUNCTION: Endoglucanase with high activity on carboxymethylcellulose
CC       (CMC) and lichenan, but not active on Avicel.
CC       {ECO:0000269|PubMed:9720200}.
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:0000269|PubMed:9720200};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by Hg(2+), Ag(+) and Fe(3+). To
CC       a lesser extent, is also inhibited by Pb(2+), Mn(2+), Sn(2+) and
CC       Cu(2+). By contrast, Ni(2+), Zn(2+), Co(2+), Ba(2+) and NH(4)(+) do not
CC       affect enzyme activity, while 10 mM Ca(2+), and Mg(2+) produce a
CC       stimulating effect. Is also strongly inhibited by chemicals such as N-
CC       bromosuccinimide and dimethyl(2-dihydroxy-5-nitrobenzyl)sulphonium
CC       bromide. Is not affected by N-acetylimidazole.
CC       {ECO:0000269|PubMed:9720200}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.0. Highly stable at acid pH. Retains 100% of its
CC         activity after 90 minutes incubation at pH 4.5 and 45 degrees
CC         Celsius, and 95% of the initial activity is found after 15 days
CC         incubation at room temperature and pH 4.5.
CC         {ECO:0000269|PubMed:9720200};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Shows 98% and 51% of its
CC         maximum activity at 45 and 55 degrees Celsius, respectively.
CC         {ECO:0000269|PubMed:9720200};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9720200}.
CC   -!- BIOTECHNOLOGY: Study of the performance of endoglucanase A on paper
CC       manufacture from agricultural fibers shows that treatment with the
CC       enzyme improves the properties of the pulp and the quality of paper.
CC       CelA treatment enhances the physical properties (stretch and tensile
CC       index) of paper from wheat straw, while dewatering properties are
CC       slightly diminished. {ECO:0000269|PubMed:9720200}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {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; Y12512; CAA73113.1; -; Genomic_DNA.
DR   AlphaFoldDB; O08342; -.
DR   SMR; O08342; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   OrthoDB; 9800955at2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000305"
FT   CHAIN           33..400
FT                   /note="Endoglucanase A"
FT                   /id="PRO_0000371421"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  44799 MW;  E89CB35BBC6F8AE5 CRC64;
     MTKTFKKFSI AGLALLFMAT AAFAGWSTKA SAADMRSLTA AQITAEMGAG WNLGNQLEAT
     VNGTPNETSW GNPTITPELI KKVKAAGFKT IRIPVSYLNY IGSAPNYTVN ASWLNRIQQV
     VDYAYNEGLY VVINMHGDGF HSIPGSWLHV NSSNQNVIRD KYQKVWQQVA TRFSAYNERL
     IFESMNEVFD GNYNNPNTSY YGNLNAYNQI FVDTVRKTGG NNNARWLLVP GWNTNIDYTV
     GNYGFVVPTD NFRSSAIPSS QKRIMISAHY YSPWDFAGEE NGNITQWGAT ATNPAKRSTW
     GQEDYLDSQF KSMYDKFVTQ GYPVVMGEFG SIDKSSYDSS NNNYRAVYAK AVTATAKKYK
     LVPVYWDNGF NGQHGFALFN RFNNTVTQQN IINAIMQGMQ
//