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G4P3P9 (G4P3P9_BACIU) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein-glutamine gamma-glutamyltransferase HAMAP-Rule MF_00727

EC=2.3.2.13 HAMAP-Rule MF_00727
Alternative name(s):
Transglutaminase HAMAP-Rule MF_00727
Gene names
Name:tgl HAMAP-Rule MF_00727 EMBL AEP92130.1
ORF Names:I33_3214 EMBL AEP92130.1
OrganismBacillus subtilis subsp. subtilis str. RO-NN-1 [Complete proteome] EMBL AEP92130.1
Taxonomic identifier1052588 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links By similarity. HAMAP-Rule MF_00727

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3. HAMAP-Rule MF_00727

Sequence similarities

Belongs to the bacillus TGase family. HAMAP-Rule MF_00727

Ontologies

Keywords
   Biological processSporulation HAMAP-Rule MF_00727
   Cellular componentCapsid protein EMBL AEP92130.1
Virion
   Molecular functionAcyltransferase HAMAP-Rule MF_00727 EMBL AEP92130.1
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processsporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentviral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein-glutamine gamma-glutamyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
G4P3P9 [UniParc].

Last modified December 14, 2011. Version 1.
Checksum: 70D3962F2332829C

FASTA24528,329
        10         20         30         40         50         60 
MIIVSGQLLR PQDIENWQID QNLNPLLKEM IETPVQFDYH SIAELMFELK LRMNIVAAAK 

        70         80         90        100        110        120 
TLHKSGAKFA TFFKTYGNTT YWRVSPEGAL ELKYRMPPSK AIRDIAENGP FYAFECATAI 

       130        140        150        160        170        180 
VVIYYLALID TIGEDKFNAS FDRIILYDWH YEKLPIYTET GHHFFLGDCL YFKNPEFDPQ 

       190        200        210        220        230        240 
KAQWRGENVI LLGEDKYFAH GLGILNGQQI IEKLNSFRKK GALQSAYLLS QATRLDVPSL 


FRIVR 

« Hide

References

[1]"Whole-genome sequences of Bacillus subtilis and close relatives."
Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A., Daugherty S., Losick R., Kolter R., Ravel J.
J. Bacteriol. 194:2378-2379(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: RO-NN-1 EMBL AEP92130.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002906 Genomic DNA. Translation: AEP92130.1.
RefSeqYP_005558104.1. NC_017195.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEP92130; AEP92130; I33_3214.
GeneID12192599.
KEGGbsr:I33_3214.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00686.

Enzyme and pathway databases

BioCycBSUB1052588:GL8O-3200-MONOMER.

Family and domain databases

HAMAPMF_00727. Tgl.
InterProIPR020916. Gln_gamma-glutamylTfrase_bac.
[Graphical view]
ProDomPD119415. PD119415. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameG4P3P9_BACIU
AccessionPrimary (citable) accession number: G4P3P9
Entry history
Integrated into UniProtKB/TrEMBL: December 14, 2011
Last sequence update: December 14, 2011
Last modified: April 16, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)