ID   GUN1_STRSS              Reviewed;         359 AA.
AC   P13933;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 3.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Endoglucanase 1;
DE            EC=3.2.1.4;
DE   AltName: Full=CMCase I;
DE   AltName: Full=Carboxymethyl cellulase;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=casA;
OS   Streptomyces sp. (strain KSM-9).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=74575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 71-95.
RX   PubMed=3410319; DOI=10.1016/0378-1119(88)90459-3;
RA   Nakai R., Horinouchi S., Beppu T.;
RT   "Cloning and nucleotide sequence of a cellulase gene, casA, from an
RT   alkalophilic Streptomyces strain.";
RL   Gene 65:229-238(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=8422992; DOI=10.1016/0378-1119(93)90547-g;
RA   Damude H.G., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.;
RT   "Endoglucanase CasA from alkalophilic Streptomyces strain KSM-9 is a
RT   typical member of family B of beta-1,4-glucanases.";
RL   Gene 123:105-107(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 185-222, AND SEQUENCE REVISION.
RX   PubMed=1761039; DOI=10.1111/j.1432-1033.1991.tb16384.x;
RA   Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A.,
RA   Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.;
RT   "Structural and functional relationships in two families of beta-1,4-
RT   glycanases.";
RL   Eur. J. Biochem. 202:367-377(1991).
CC   -!- FUNCTION: CMCase I preferentially hydrolyzes carboxymethyl cellulose
CC       (CMC).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) 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; L03218; AAA26713.1; -; Genomic_DNA.
DR   EMBL; X61008; CAA43330.1; -; Genomic_DNA.
DR   EMBL; M20921; AAA26776.1; ALT_SEQ; Genomic_DNA.
DR   PIR; JN0544; JN0544.
DR   PIR; JT0308; JT0308.
DR   AlphaFoldDB; P13933; -.
DR   SMR; P13933; -.
DR   CAZy; GH6; Glycoside Hydrolase Family 6.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.40; -; 1.
DR   InterPro; IPR016288; Beta_cellobiohydrolase.
DR   InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR   InterPro; IPR001524; Glyco_hydro_6_CS.
DR   PANTHER; PTHR34876; PTHR34876; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   SUPFAM; SSF51989; SSF51989; 1.
DR   PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..?
FT   PROPEP          ?..70
FT                   /evidence="ECO:0000269|PubMed:3410319"
FT                   /id="PRO_0000007907"
FT   CHAIN           71..359
FT                   /note="Endoglucanase 1"
FT                   /id="PRO_0000007908"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT   DISULFID        155..199
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   359 AA;  36515 MW;  F1300238834E906C CRC64;
     MENPRTTPTP TPLRRRRSER RARGGRVLTA LTGVTLLAGL AIAPAATGAS PSPAPPASPA
     PSADSGTADA GTTALPSMEL YRAEAGVHAW LDANPGDHRA PLIAERIGSQ PQAVWFAGAY
     NPGTITQQVA EVTSAAAAAG QLPVVVPYMI PFRDCGNHSG GGAPSFAAYA EWSGLFAAGL
     GSEPVVVVLE PDAIPLIDCL DNQQRAERLA ALAGLAEAVT DANPEARVYY DVGHSAWHAP
     AAIAPTLVEA GILEHGAGIA TNISNYRTTT DETAYASAVI AELGGGLGAV VDTSRNGNGP
     LGSEWCDPPG RLVGNNPTVN PGVPGVDAFL WIKLPGELDG CDGPVGSFSP AKAYELAGG