ID   GUNV_PECCC              Reviewed;         505 AA.
AC   Q47096;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Endoglucanase 5;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase V;
DE   AltName: Full=Endo-1,4-beta-glucanase V;
DE   AltName: Full=Endoglucanase V;
DE   Flags: Precursor;
GN   Name=celV;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=8246888; DOI=10.1007/bf00284687;
RA   Cooper V.J.C., Salmond G.P.C.;
RT   "Molecular analysis of the major cellulase (CelV) of Erwinia carotovora:
RT   evidence for an evolutionary 'mix-and-match' of enzyme domains.";
RL   Mol. Gen. Genet. 241:341-350(1993).
CC   -!- FUNCTION: Endoglucanase with some exoglucanase activity.
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 about 7.0.;
CC       Temperature dependence:
CC         Optimum temperature is about 42 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; X76000; CAA53592.1; -; Genomic_DNA.
DR   PIR; S39962; S39962.
DR   AlphaFoldDB; Q47096; -.
DR   SMR; Q47096; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 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   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51172; CBM3; 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..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..505
FT                   /note="Endoglucanase 5"
FT                   /id="PRO_0000007858"
FT   DOMAIN          353..505
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   REGION          32..334
FT                   /note="Catalytic"
FT   REGION          332..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..352
FT                   /note="Linker"
FT   COMPBIAS        337..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   ACT_SITE        256
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         68..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         262..263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         295..297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
SQ   SEQUENCE   505 AA;  54900 MW;  DBEA9337BB4D2623 CRC64;
     MWMRRNQIVR KLTLGVVTTV LGMSLSFSAL SATPVETHGQ LSIENGRLVD EQGKRVQLRG
     ISSHGLQWFG DYVNKDSMKW LRDDWGINVF RVAMYTAADG YISNPSLANK VKEAVAAAQS
     LGVYIIIDWH ILSDNDPNIY KAQAKTFFAE MAGLYGSSPN VIYEIANEPN GGVTWNGQIR
     PYALEVTDTI RSKDPDNLII VGTGTWSQDI HDAADNQLPD PNTMYALHFY AGTHGQFLRD
     RIDYAQSRGA AIFVSEWGTS DASGNGGPFL PESQTWIDFL NNRGVSWVNW SLTDKSEASA
     ALAPGASKSG GWTEQNLSTS GKFVREQIRA GANLGGGDTP TTPTEPTNPG NGTTGDVVLQ
     YRNVDNNPSD DAIRMAVNIK NTGSTPIKLS DLQVRYYFHD DGKPGANLFV DWANVGPNNI
     VTSTGTPAAS TDKANRYVLV TFSSGAGSLQ PGAETGEVQV RIHAGDWSNV NETNDYSYGA
     NVTSYANWDK ITVHDKGTLV WGVEP