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P17974 (GUN_RALSL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene names
Name:egl
OrganismRalstonia solanacearum (Pseudomonas solanacearum)
Taxonomic identifier305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Subcellular location

Cell membrane; Lipid-anchor Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMLipoprotein
Palmitate
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Propeptide20 – 4526
PRO_0000007869
Chain46 – 426381Endoglucanase
PRO_0000007870

Sites

Active site2491Proton donor By similarity
Active site3611Nucleophile By similarity

Amino acid modifications

Lipidation201N-palmitoyl cysteine Ref.3
Lipidation201S-diacylglycerol cysteine

Sequences

Sequence LengthMass (Da)Tools
P17974 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: 51E13AD4442CF4A8

FASTA42645,578
        10         20         30         40         50         60 
MRRCMPLVAA SVAALMLAGC GGGDGDPSLS TASVSATDTT TLKPAATSTT SSVWLTLAKD 

        70         80         90        100        110        120 
SAAFTVSGTR TVRYGAGSAW VEKSVSGSGR CTSTFFGKDP AAGVAKVCQL LQGTGTLLWR 

       130        140        150        160        170        180 
GVSLAGAEFG EGSLPGTYGS NYIYPSADSV TYYKNKGMNL VRLPFRWERL QPTLNQVFDA 

       190        200        210        220        230        240 
NELSRLTGFV NAVTATGQTV LLDPHNYARY YGNVIGSSAV PNSAYADFWR RLATQFKSNP 

       250        260        270        280        290        300 
RVILGLMNEP NSMPTEQWLS GANAELAAIR SANASNVVFV PGNAWTGAHS WNQNWYGTPN 

       310        320        330        340        350        360 
GTVMKGINDP GHNLVFEVHQ YLDGDSSGQS ANCVSATIGA QRLQDFTTWL RSNGYRGFLG 

       370        380        390        400        410        420 
EFGAASNDTC NQAVSNMLTF VKNNADVWTG WAWWAGGPWW GGYMYSIEPS NGVDKPQMSV 


LAPYLK 

« Hide

References

[1]"Role of the two-component leader sequence and mature amino acid sequences in extracellular export of endoglucanase EGL from Pseudomonas solanacearum."
Huang J., Schell M.A.
J. Bacteriol. 174:1314-1323(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AW.
[2]"Excretion of the egl gene product of Pseudomonas solanacearum."
Huang J., Sukordhaman M., Schell M.A.
J. Bacteriol. 171:3767-3774(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112, PARTIAL PROTEIN SEQUENCE.
[3]"Evidence that extracellular export of the endoglucanase encoded by egl of Pseudomonas solanacearum occurs by a two-step process involving a lipoprotein intermediate."
Huang J., Schell M.A.
J. Biol. Chem. 265:11628-11632(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84922 Genomic DNA. Translation: AAA61980.1.
PIRA42649.

3D structure databases

ProteinModelPortalP17974.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN_RALSL
AccessionPrimary (citable) accession number: P17974
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries