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P22222

- E13B_CELCE

UniProt

P22222 - E13B_CELCE

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Protein

Glucan endo-1,3-beta-glucosidase

Gene
N/A
Organism
Cellulosimicrobium cellulans (Arthrobacter luteus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Lysis of cellular walls containing beta-1,3-glucans. Implicated in the defense against fungal pathogens.

Catalytic activityi

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Keywords - Ligandi

Lectin

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH64. Glycoside Hydrolase Family 64.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan endo-1,3-beta-glucosidase (EC:3.2.1.39)
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name:
(1->3)-beta-glucanase
OrganismiCellulosimicrobium cellulans (Arthrobacter luteus)
Taxonomic identifieri1710 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaePromicromonosporaceaeCellulosimicrobium

Subcellular locationi

Periplasm 1 Publication

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Tat-type signal1 PublicationPROSITE-ProRule annotationAdd
BLAST
Chaini37 – 548512Glucan endo-1,3-beta-glucosidasePRO_0000012235Add
BLAST

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Structurei

3D structure databases

ProteinModelPortaliP22222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini422 – 548127Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 430394Possess beta-glucanase activity, but is unable to lyse viable cellsAdd
BLAST
Regioni472 – 54877Essential for the lytic activity, but not for the beta-glucanase functionAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 64 family.Curated
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR000772. Ricin_B_lectin.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P22222-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPHDRKNSSR RAWAALCAAV LAVSGALVGV AAPASAVPAT IPLTITNDSG
60 70 80 90 100
RGPIYLYVLG ERDGVAGWAD AGGTFHPWPG GVGPVPVPAP DASIAGPGPG
110 120 130 140 150
QSVTIRLPKL SGRVYYSYGQ KMTFQIVLDG RLVQPAVQND SDPNRNILFN
160 170 180 190 200
WTEYTLNDGG LWINSTQVDH WSAPYQVGVQ RADGQVLSTG MLKPNGYEAF
210 220 230 240 250
YTALEGAGWG GLVQRAPDGS RLRALNPSHG IDVGKISSAS IDSYVTEVWN
260 270 280 290 300
SYRTRDMVVT PFSHEPGTQF RGRVDGDWFR FRSGSGQEVA AFKKPDASSV
310 320 330 340 350
YGCHKDLQAP NDHVVGPIAR TLCAALVRTT ALTNPNQPDA NSAGFYQDAR
360 370 380 390 400
TNVYAKLAHQ QMANGKAYAF AFDDVGAHES LVHDGNPQAA YIKLDPFTGT
410 420 430 440 450
ATPLGNGGST EQPGTPGGLP AGTGALRIGS TLCLDVPWAD PTDTNQVQLA
460 470 480 490 500
TCSGNAAQQW TRGTDGTVRA LGKCLDVARS GTADGTAVWI YTCNGTGAQK
510 520 530 540
WTYDSATKAL RNPQSGKCLD AQGGAPLRDG QKVQLWTCNQ TEAQRWTL
Length:548
Mass (Da):58,089
Last modified:August 1, 1991 - v1
Checksum:i412B5A4AA24C048D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60826 Genomic DNA. Translation: AAA25520.1.
PIRiA39094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60826 Genomic DNA. Translation: AAA25520.1 .
PIRi A39094.

3D structure databases

ProteinModelPortali P22222.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GH64. Glycoside Hydrolase Family 64.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR000772. Ricin_B_lectin.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary sequence of the glucanase gene from Oerskovia xanthineolytica. Expression and purification of the enzyme from Escherichia coli."
    Shen S.-H., Chretien P., Bastien L., Slilaty S.N.
    J. Biol. Chem. 266:1058-1063(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-63, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiE13B_CELCE
AccessioniPrimary (citable) accession number: P22222
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 29, 2014
This is version 78 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

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