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P10475

- GUN2_BACSU

UniProt

P10475 - GUN2_BACSU

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Protein

Endoglucanase

Gene

eglS

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP10475.
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

        10         20         30         40         50
MKRSISIFIT CLLITLLTMG GMIASPASAA GTKTPVAKNG QLSIKGTQLV
60 70 80 90 100
NRDGKAVQLK GISSHGLQWY GEYVNKDSLK WLRDDWGITV FRAAMYTADG
110 120 130 140 150
GYIDNPSVKN KVKEAVEAAK ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK
160 170 180 190 200
EMSSLYGNTP NVIYEIANEP NGDVNWKRDI KPYAEEVISV IRKNDPDNII
210 220 230 240 250
IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQFLR DKANYALSKG
260 270 280 290 300
APIFVTEWGT SDASGNGGVF LDQSREWLKY LDSKTISWVN WNLSDKQESS
310 320 330 340 350
SALKPGASKT GGWRLSDLSA SGTFVRENIL GTKDSTKDIP ETPSKDKPTQ
360 370 380 390 400
ENGISVQYRA GDGSMNSNQI RPQLQIKNNG NTTVDLKDVT ARYWYKAKNK
410 420 430 440 450
GQNFDCDYAQ IGCGNVTHKF VTLHKPKQGA DTYLELGFKN GTLAPGASTG
460 470 480 490
NIQLRLHNDD WSNYAQSGDY SFFKSNTFKT TKKITLYDQG KLIWGTEPN
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. Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P10475.
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: November 26, 2014
This is version 128 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