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P17974

- GUN_RALSL

UniProt

P17974 - GUN_RALSL

Protein

Endoglucanase

Gene

egl

Organism
Ralstonia solanacearum (Pseudomonas solanacearum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (01 May 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei249 – 2491Proton donorBy similarity
    Active sitei361 – 3611NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase (EC:3.2.1.4)
    Alternative name(s):
    Cellulase
    Endo-1,4-beta-glucanase
    Gene namesi
    Name:egl
    OrganismiRalstonia solanacearum (Pseudomonas solanacearum)
    Taxonomic identifieri305 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Add
    BLAST
    Propeptidei20 – 4526PRO_0000007869Add
    BLAST
    Chaini46 – 426381EndoglucanasePRO_0000007870Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi20 – 201N-palmitoyl cysteine1 PublicationPROSITE-ProRule annotation
    Lipidationi20 – 201S-diacylglycerol cysteine1 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Lipoprotein, Palmitate, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliP17974.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17974-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRCMPLVAA SVAALMLAGC GGGDGDPSLS TASVSATDTT TLKPAATSTT    50
    SSVWLTLAKD SAAFTVSGTR TVRYGAGSAW VEKSVSGSGR CTSTFFGKDP 100
    AAGVAKVCQL LQGTGTLLWR GVSLAGAEFG EGSLPGTYGS NYIYPSADSV 150
    TYYKNKGMNL VRLPFRWERL QPTLNQVFDA NELSRLTGFV NAVTATGQTV 200
    LLDPHNYARY YGNVIGSSAV PNSAYADFWR RLATQFKSNP RVILGLMNEP 250
    NSMPTEQWLS GANAELAAIR SANASNVVFV PGNAWTGAHS WNQNWYGTPN 300
    GTVMKGINDP GHNLVFEVHQ YLDGDSSGQS ANCVSATIGA QRLQDFTTWL 350
    RSNGYRGFLG EFGAASNDTC NQAVSNMLTF VKNNADVWTG WAWWAGGPWW 400
    GGYMYSIEPS NGVDKPQMSV LAPYLK 426
    Length:426
    Mass (Da):45,578
    Last modified:May 1, 1992 - v2
    Checksum:i51E13AD4442CF4A8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84922 Genomic DNA. Translation: AAA61980.1.
    PIRiA42649.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84922 Genomic DNA. Translation: AAA61980.1 .
    PIRi A42649.

    3D structure databases

    ProteinModelPortali P17974.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiGUN_RALSL
    AccessioniPrimary (citable) accession number: P17974
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3