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P10475

- GUN2_BACSU

UniProt

P10475 - GUN2_BACSU

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Protein
Endoglucanase
Gene
eglS, bglC, gld, BSU18130
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 donor By similarity
Active sitei257 – 2571Nucleophile By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

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 Publication
Add
BLAST
Chaini30 – 499470Endoglucanase
PRO_0000007840Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU18130.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP10475.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini350 – 499150CBM3
Add
BLAST

Sequence similaritiesi

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti283 – 2831S → N in CAA47429. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 125 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

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