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P10475

- GUN2_BACSU

UniProt

P10475 - GUN2_BACSU

Protein

Endoglucanase

Gene

eglS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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 sitei169 – 1691Proton donorBy similarity
    Active sitei257 – 2571NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciBSUB:BSU18130-MONOMER.

    Protein family/group databases

    CAZyiCBM3. Carbohydrate-Binding Module Family 3.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase (EC:3.2.1.4)
    Alternative name(s):
    Carboxymethyl-cellulase
    Short name:
    CMCase
    Short name:
    Cellulase
    Endo-1,4-beta-glucanase
    Gene namesi
    Name:eglS
    Synonyms:bglC, gld
    Ordered Locus Names:BSU18130
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU18130. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29291 PublicationAdd
    BLAST
    Chaini30 – 499470EndoglucanasePRO_0000007840Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU18130.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 394
    Beta strandi43 – 453
    Beta strandi48 – 503
    Beta strandi60 – 656
    Helixi67 – 704
    Helixi71 – 733
    Helixi76 – 8510
    Beta strandi89 – 9810
    Turni102 – 1043
    Helixi106 – 1083
    Helixi109 – 12214
    Beta strandi125 – 1317
    Beta strandi133 – 1353
    Turni138 – 1414
    Helixi142 – 15615
    Beta strandi162 – 1654
    Turni176 – 1794
    Helixi180 – 19415
    Beta strandi196 – 1983
    Beta strandi200 – 2023
    Helixi205 – 2084
    Helixi211 – 2155
    Beta strandi224 – 2318
    Turni232 – 2343
    Helixi237 – 24812
    Beta strandi253 – 2619
    Helixi271 – 28313
    Beta strandi288 – 2947
    Helixi315 – 3173
    Helixi320 – 33011
    Beta strandi355 – 3606
    Beta strandi373 – 3775
    Helixi386 – 3883
    Beta strandi389 – 3957
    Beta strandi403 – 4097
    Beta strandi417 – 4226
    Beta strandi427 – 4293
    Beta strandi432 – 4387
    Beta strandi447 – 4504
    Beta strandi452 – 4576
    Turni466 – 4738
    Beta strandi484 – 4885
    Beta strandi491 – 4944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L8ANMR-A354-499[»]
    3PZTX-ray1.97A/B27-332[»]
    3PZUX-ray2.10A/B27-332[»]
    3PZVX-ray2.87A/B/C/D27-332[»]
    ProteinModelPortaliP10475.
    SMRiP10475. Positions 36-329, 353-498.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10475.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini350 – 499150CBM3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000253566.
    KOiK01179.
    OMAiKGISSHG.
    OrthoDBiEOG6NSGCN.

    Family and domain databases

    Gene3Di2.60.40.710. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00942. CBM_3. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SMARTiSM01067. CBM_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51172. CBM3. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10475-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRSISIFIT CLLITLLTMG GMIASPASAA GTKTPVAKNG QLSIKGTQLV    50
    NRDGKAVQLK GISSHGLQWY GEYVNKDSLK WLRDDWGITV FRAAMYTADG 100
    GYIDNPSVKN KVKEAVEAAK ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK 150
    EMSSLYGNTP NVIYEIANEP NGDVNWKRDI KPYAEEVISV IRKNDPDNII 200
    IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQFLR DKANYALSKG 250
    APIFVTEWGT SDASGNGGVF LDQSREWLKY LDSKTISWVN WNLSDKQESS 300
    SALKPGASKT GGWRLSDLSA SGTFVRENIL GTKDSTKDIP ETPSKDKPTQ 350
    ENGISVQYRA GDGSMNSNQI RPQLQIKNNG NTTVDLKDVT ARYWYKAKNK 400
    GQNFDCDYAQ IGCGNVTHKF VTLHKPKQGA DTYLELGFKN GTLAPGASTG 450
    NIQLRLHNDD WSNYAQSGDY SFFKSNTFKT TKKITLYDQG KLIWGTEPN 499
    Length:499
    Mass (Da):55,287
    Last modified:July 1, 1989 - v1
    Checksum:i8F735FF711B3EAE2
    GO

    Sequence cautioni

    The sequence CAA97610.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti283 – 2831S → N in CAA47429. (PubMed:7710280)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29076 Genomic DNA. Translation: CAA82317.1.
    X04689 Genomic DNA. Translation: CAA28392.1.
    X67044 Genomic DNA. Translation: CAA47429.1.
    Z73234 Genomic DNA. Translation: CAA97610.1. Different initiation.
    AL009126 Genomic DNA. Translation: CAB13696.2.
    PIRiG69593.
    RefSeqiNP_389695.2. NC_000964.3.
    WP_003231540.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB13696; CAB13696; BSU18130.
    GeneIDi938607.
    KEGGibsu:BSU18130.
    PATRICi18975461. VBIBacSub10457_1922.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29076 Genomic DNA. Translation: CAA82317.1 .
    X04689 Genomic DNA. Translation: CAA28392.1 .
    X67044 Genomic DNA. Translation: CAA47429.1 .
    Z73234 Genomic DNA. Translation: CAA97610.1 . Different initiation.
    AL009126 Genomic DNA. Translation: CAB13696.2 .
    PIRi G69593.
    RefSeqi NP_389695.2. NC_000964.3.
    WP_003231540.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L8A NMR - A 354-499 [» ]
    3PZT X-ray 1.97 A/B 27-332 [» ]
    3PZU X-ray 2.10 A/B 27-332 [» ]
    3PZV X-ray 2.87 A/B/C/D 27-332 [» ]
    ProteinModelPortali P10475.
    SMRi P10475. Positions 36-329, 353-498.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU18130.

    Protein family/group databases

    CAZyi CBM3. Carbohydrate-Binding Module Family 3.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13696 ; CAB13696 ; BSU18130 .
    GeneIDi 938607.
    KEGGi bsu:BSU18130.
    PATRICi 18975461. VBIBacSub10457_1922.

    Organism-specific databases

    GenoListi BSU18130. [Micado ]

    Phylogenomic databases

    HOGENOMi HOG000253566.
    KOi K01179.
    OMAi KGISSHG.
    OrthoDBi EOG6NSGCN.

    Enzyme and pathway databases

    BioCyci BSUB:BSU18130-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P10475.

    Family and domain databases

    Gene3Di 2.60.40.710. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00942. CBM_3. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SMARTi SM01067. CBM_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51172. CBM3. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: PAP115.
    2. "Nucleotide sequence of an endo-beta-1,4-glucanase gene from Bacillus subtilis CK-2."
      Lindahl V., Aa K., Tronsmo A.
      Antonie Van Leeuwenhoek 66:327-332(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CK-2.
    3. "New genes in the 170 degrees region of the Bacillus subtilis genome encode DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid transporter."
      Rose M., Entian K.-D.
      Microbiology 142:3097-3101(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    4. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    5. "Characterization of production and enzyme properties of an endo-beta-1,4-glucanase from Bacillus subtilis CK-2 isolated from compost soil."
      Aa K., Flengsrud R., Lindahl V., Tronsmo A.
      Antonie Van Leeuwenhoek 66:319-326(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-45.
      Strain: CK-2.

    Entry informationi

    Entry nameiGUN2_BACSU
    AccessioniPrimary (citable) accession number: P10475
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3