ID   GUNC_RUMCH              Reviewed;         460 AA.
AC   P37699; B8I7V2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Endoglucanase C;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase C;
DE   AltName: Full=EGCCC;
DE   AltName: Full=Endo-1,4-beta-glucanase C;
DE   Flags: Precursor;
GN   Name=celCCC; OrderedLocusNames=Ccel_0730;
OS   Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10) (Clostridium cellulolyticum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=394503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RX   PubMed=1398087; DOI=10.1016/0378-1119(92)90062-t;
RA   Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T.,
RA   Belaich J.-P.;
RT   "Sequence analysis of a gene cluster encoding cellulases from Clostridium
RT   cellulolyticum.";
RL   Gene 119:17-28(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 33-37, AND CHARACTERIZATION.
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RX   PubMed=8223599; DOI=10.1111/j.1432-1033.1993.tb18277.x;
RA   Fierobe H.-P., Bagnara-Tardif C., Gaudin C., Guerlesquin F., Sauve P.,
RA   Belaich A., Belaich J.-P.;
RT   "Purification and characterization of endoglucanase C from Clostridium
RT   cellulolyticum. Catalytic comparison with endoglucanase A.";
RL   Eur. J. Biochem. 217:557-565(1993).
CC   -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC       requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC       cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC       cut the disaccharide cellobiose from the non-reducing end of the
CC       cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC       cellobiose and other short cello-oligosaccharides to glucose.
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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SUBUNIT: Monomer.
CC   -!- PTM: There are two forms of the cellulase. The shorter form lacks
CC       probably the C-terminal reiterated domains.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC       {ECO:0000305}.
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DR   EMBL; M87018; AAA73867.1; -; Genomic_DNA.
DR   EMBL; CP001348; ACL75109.1; -; Genomic_DNA.
DR   PIR; JC1299; JC1299.
DR   RefSeq; WP_015924276.1; NC_011898.1.
DR   AlphaFoldDB; P37699; -.
DR   SMR; P37699; -.
DR   STRING; 394503.Ccel_0730; -.
DR   CAZy; GH8; Glycoside Hydrolase Family 8.
DR   KEGG; cce:Ccel_0730; -.
DR   eggNOG; COG3405; Bacteria.
DR   HOGENOM; CLU_036185_0_0_9; -.
DR   OrthoDB; 9803461at2; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001349; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd14256; Dockerin_I; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002037; Glyco_hydro_8.
DR   InterPro; IPR019834; Glyco_hydro_8_CS.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   PRINTS; PR00735; GLHYDRLASE8.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:8223599"
FT   CHAIN           33..460
FT                   /note="Endoglucanase C"
FT                   /id="PRO_0000007936"
FT   DOMAIN          400..460
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10058"
FT   CONFLICT        91
FT                   /note="S -> T (in Ref. 1; AAA73867)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   460 AA;  50483 MW;  2F31E1F6CB41504F CRC64;
     MIKGSSLKRF KSLVMAAIFS VSIISTAIAS SAADQIPFPY DAKYPNGAYS CLADSQSIGN
     NLVRSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG LGYGLLLSVY FGEQQLFDDL
     YRYVKVFLNS NGLMSWRIDS SGNIMGKDSI GAATDADEDI AVSLVFAHKK WGTSGGFNYQ
     TEAKNYINNI YNKMVEPGTY VIKAGDTWGG SNVTNPSYFA PAWYRIFADF TGNSGWINVA
     NKCYEIADKA RNSNTGLVPD WCTANGTPAS GQGFDFYYDA IRYQWRAAID YSWYGTAKAK
     THCDAISNFF KNIGYANIKD GYTISGSQIS SNHTATFVSC AAAAAMTGTD TTYAKNIYNE
     CVKVKDSGNY TYFGNTLRMM VLLYTTGNFP NLYTYNSQPK PDLKGDVNND GAIDALDIAA
     LKKAILTQTT SNISLTNADM NNDGNIDAID FAQLKVKLLN
//