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J3UUU9

- J3UUU9_BACTU

UniProt

J3UUU9 - J3UUU9_BACTU

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Protein

Protein-glutamine gamma-glutamyltransferase

Gene

tgl

Organism
Bacillus thuringiensis HD-771
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links.UniRule annotation

Catalytic activityi

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.UniRule annotation

GO - Molecular functioni

  1. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. sporulation resulting in formation of a cellular spore Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationImported, Transferase

Keywords - Biological processi

SporulationUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-glutamine gamma-glutamyltransferaseUniRule annotation (EC:2.3.2.13UniRule annotation)
Alternative name(s):
TransglutaminaseUniRule annotation
Gene namesi
Name:tglUniRule annotationImported
ORF Names:BTG_29615Imported
OrganismiBacillus thuringiensis HD-771Imported
Taxonomic identifieri1218175 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000005259: Chromosome

Family & Domainsi

Sequence similaritiesi

Belongs to the bacillus TGase family.UniRule annotation

Phylogenomic databases

KOiK00686.

Family and domain databases

HAMAPiMF_00727. Tgl.
InterProiIPR020916. Gln_gamma-glutamylTfrase_bac.
[Graphical view]
ProDomiPD119415. PD119415. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

J3UUU9-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MIVIGRSIVH PYITNEYEPF VAEKQQILSI MAGNQEVYSF RTADELSFDL
60 70 80 90 100
NLRVNIIISA LELFQSGFQF RTFQQSFCNP QYWKRTSLGG FELLPNIPPS
110 120 130 140 150
IAIQDIFKNG KLYGTECATA MIIIFYKALL SLYEEETFNR LFANLLLYTW
160 170 180 190 200
DYDQDLRLIT KTGGDLVPGD LVYFKNPQVN PSTIEWQGEN TIYLGNFFFY
210 220 230 240 250
GHGVGVKTKE EIIYSLNERR VPYAFISAFL TDTITRIDSR IMSQYASSST
260 270
PQTSISFIPI RDDAIVATVG HTTTIY
Length:276
Mass (Da):31,578
Last modified:October 31, 2012 - v1
Checksum:iA490D858F1C47794
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003752 Genomic DNA. Translation: AFQ19316.1.
RefSeqiYP_006607349.1. NC_018500.1.

Genome annotation databases

EnsemblBacteriaiAFQ19316; AFQ19316; BTG_29615.
GeneIDi13498576.
KEGGibti:BTG_29615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003752 Genomic DNA. Translation: AFQ19316.1 .
RefSeqi YP_006607349.1. NC_018500.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFQ19316 ; AFQ19316 ; BTG_29615 .
GeneIDi 13498576.
KEGGi bti:BTG_29615.

Phylogenomic databases

KOi K00686.

Family and domain databases

HAMAPi MF_00727. Tgl.
InterProi IPR020916. Gln_gamma-glutamylTfrase_bac.
[Graphical view ]
ProDomi PD119415. PD119415. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

  1. Doggett N., Teshima H., Bruce D., Detter J.C., Johnson S.L., Han C.
    Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: HD-771Imported.

Entry informationi

Entry nameiJ3UUU9_BACTU
AccessioniPrimary (citable) accession number: J3UUU9
Entry historyi
Integrated into UniProtKB/TrEMBL: October 31, 2012
Last sequence update: October 31, 2012
Last modified: October 1, 2014
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3