GUN_RALSL
ID GUN_RALSL Reviewed; 426 AA.
AC P17974;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Endoglucanase;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor;
GN Name=egl;
OS Ralstonia solanacearum (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AW;
RX PubMed=1735723; DOI=10.1128/jb.174.4.1314-1323.1992;
RA Huang J., Schell M.A.;
RT "Role of the two-component leader sequence and mature amino acid sequences
RT in extracellular export of endoglucanase EGL from Pseudomonas
RT solanacearum.";
RL J. Bacteriol. 174:1314-1323(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2738021; DOI=10.1128/jb.171.7.3767-3774.1989;
RA Huang J., Sukordhaman M., Schell M.A.;
RT "Excretion of the egl gene product of Pseudomonas solanacearum.";
RL J. Bacteriol. 171:3767-3774(1989).
RN [3]
RP PROTEOLYTIC PROCESSING, DIACYLGLYCEROL AT CYS-20, AND PALMITOYLATION AT
RP CYS-20.
RX PubMed=2195024; DOI=10.1016/s0021-9258(19)38444-3;
RA Huang J., Schell M.A.;
RT "Evidence that extracellular export of the endoglucanase encoded by egl of
RT Pseudomonas solanacearum occurs by a two-step process involving a
RT lipoprotein intermediate.";
RL J. Biol. Chem. 265:11628-11632(1990).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; M84922; AAA61980.1; -; Genomic_DNA.
DR PIR; A42649; A42649.
DR AlphaFoldDB; P17974; -.
DR SMR; P17974; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR GO; GO:0005886; C:plasma membrane; 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 InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Polysaccharide degradation; Signal; Zymogen.
FT SIGNAL 1..19
FT PROPEP 20..45
FT /id="PRO_0000007869"
FT CHAIN 46..426
FT /note="Endoglucanase"
FT /id="PRO_0000007870"
FT ACT_SITE 249
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:2195024"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:2195024"
SQ SEQUENCE 426 AA; 45578 MW; 51E13AD4442CF4A8 CRC64;
MRRCMPLVAA SVAALMLAGC GGGDGDPSLS TASVSATDTT TLKPAATSTT SSVWLTLAKD
SAAFTVSGTR TVRYGAGSAW VEKSVSGSGR CTSTFFGKDP AAGVAKVCQL LQGTGTLLWR
GVSLAGAEFG EGSLPGTYGS NYIYPSADSV TYYKNKGMNL VRLPFRWERL QPTLNQVFDA
NELSRLTGFV NAVTATGQTV LLDPHNYARY YGNVIGSSAV PNSAYADFWR RLATQFKSNP
RVILGLMNEP NSMPTEQWLS GANAELAAIR SANASNVVFV PGNAWTGAHS WNQNWYGTPN
GTVMKGINDP GHNLVFEVHQ YLDGDSSGQS ANCVSATIGA QRLQDFTTWL RSNGYRGFLG
EFGAASNDTC NQAVSNMLTF VKNNADVWTG WAWWAGGPWW GGYMYSIEPS NGVDKPQMSV
LAPYLK