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Protein

Endoglucanase

Gene

eglS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei169Proton donorBy similarity1
Active sitei257NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000000784030 – 499EndoglucanaseAdd BLAST470

Proteomic databases

PaxDbiP10475.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009986.

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 39Combined sources4
Beta strandi43 – 45Combined sources3
Beta strandi48 – 50Combined sources3
Beta strandi60 – 65Combined sources6
Helixi67 – 70Combined sources4
Helixi71 – 73Combined sources3
Helixi76 – 85Combined sources10
Beta strandi89 – 98Combined sources10
Turni102 – 104Combined sources3
Helixi106 – 108Combined sources3
Helixi109 – 122Combined sources14
Beta strandi125 – 131Combined sources7
Beta strandi133 – 135Combined sources3
Turni138 – 141Combined sources4
Helixi142 – 156Combined sources15
Beta strandi162 – 165Combined sources4
Turni176 – 179Combined sources4
Helixi180 – 194Combined sources15
Beta strandi196 – 198Combined sources3
Beta strandi200 – 202Combined sources3
Helixi205 – 208Combined sources4
Helixi211 – 215Combined sources5
Beta strandi224 – 231Combined sources8
Turni232 – 234Combined sources3
Helixi237 – 248Combined sources12
Beta strandi253 – 261Combined sources9
Helixi271 – 283Combined sources13
Beta strandi288 – 294Combined sources7
Helixi315 – 317Combined sources3
Helixi320 – 330Combined sources11
Beta strandi355 – 360Combined sources6
Beta strandi373 – 377Combined sources5
Helixi386 – 388Combined sources3
Beta strandi389 – 395Combined sources7
Beta strandi403 – 409Combined sources7
Beta strandi417 – 422Combined sources6
Beta strandi427 – 429Combined sources3
Beta strandi432 – 438Combined sources7
Beta strandi447 – 450Combined sources4
Beta strandi452 – 457Combined sources6
Turni466 – 473Combined sources8
Beta strandi484 – 488Combined sources5
Beta strandi491 – 494Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10475.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini350 – 499CBM3PROSITE-ProRule annotationAdd BLAST150

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107QWR. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000253566.
InParanoidiP10475.
KOiK01179.
OMAiNEPNGDV.

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti283S → N in CAA47429 (PubMed:7710280).Curated1

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_JNCM01000035.1.

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.
PIRiG69593.
RefSeqiNP_389695.2. NC_000964.3.
WP_003231540.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009986.

Protein family/group databases

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

Proteomic databases

PaxDbiP10475.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4107QWR. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000253566.
InParanoidiP10475.
KOiK01179.
OMAiNEPNGDV.

Enzyme and pathway databases

BioCyciBSUB:BSU18130-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP10475.

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]
ProtoNetiSearch...

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 2, 2016
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.