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Protein

Protein-glutamine gamma-glutamyltransferase

Gene

tgl

Organism
Bacillus atrophaeus (strain 1942)
Status
Unreviewed-Annotation score: 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

Enzyme and pathway databases

BioCyciBATR720555:GHTA-2711-MONOMER.

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
Ordered Locus Names:BATR1942_13460Imported
OrganismiBacillus atrophaeus (strain 1942)Imported
Taxonomic identifieri720555 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000006867 Componenti: Chromosome

Family & Domainsi

Sequence similaritiesi

Belongs to the bacillus TGase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000262157.
KOiK00686.
OMAiYAFECAT.

Family and domain databases

HAMAPiMF_00727. Tgl.
InterProiIPR020916. Gln_gamma-glutamylTfrase_bac.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E3E3W7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIVSGQWLR PQDTANWQIE EGLHPLLNEM IASPIQFDYN SVAELIFELN
60 70 80 90 100
IRKNIVASAR ALHQSGAKFA TFVKTYGNKA FWRVSPEGAL ELKYKMPPSK
110 120 130 140 150
AIRDIFENGT FYAFECATAI VVIYYMAVLK TIGDDRFDLN FQRITLYDWH
160 170 180 190 200
YEKLPIYTEA GRDFVIGDCL YFNNPDFNPQ KAQWRGENVI LLEKDLYFAH
210 220 230 240
GLGILSGEKI IEKLNSFRKK DAVQSAYLLA QATRLDIPSL YRMMH
Length:245
Mass (Da):28,279
Last modified:January 11, 2011 - v1
Checksum:i65BEDA4FE393A692
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002207 Genomic DNA. Translation: ADP33614.1.
RefSeqiYP_003974545.1. NC_014639.1.

Genome annotation databases

EnsemblBacteriaiADP33614; ADP33614; BATR1942_13460.
KEGGibae:BATR1942_13460.
PATRICi42572282. VBIBacAtr152324_2729.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002207 Genomic DNA. Translation: ADP33614.1.
RefSeqiYP_003974545.1. NC_014639.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADP33614; ADP33614; BATR1942_13460.
KEGGibae:BATR1942_13460.
PATRICi42572282. VBIBacAtr152324_2729.

Phylogenomic databases

HOGENOMiHOG000262157.
KOiK00686.
OMAiYAFECAT.

Enzyme and pathway databases

BioCyciBATR720555:GHTA-2711-MONOMER.

Family and domain databases

HAMAPiMF_00727. Tgl.
InterProiIPR020916. Gln_gamma-glutamylTfrase_bac.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genomic signatures of strain selection and enhancement in Bacillus atrophaeus subsp. Globigii, a historical biowarfare simulant."
    Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D., Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.
    , Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S., Rosenzweig C.N., Skowronski E.
    Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1942Imported.

Entry informationi

Entry nameiE3E3W7_BACA1
AccessioniPrimary (citable) accession number: E3E3W7
Entry historyi
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: April 1, 2015
This is version 24 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

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 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.