GenomeNet

Database: UniProt/TrEMBL
Entry: J3UUU9_BACTU
LinkDB: J3UUU9_BACTU
Original site: J3UUU9_BACTU 
ID   J3UUU9_BACTU            Unreviewed;       276 AA.
AC   J3UUU9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-SEP-2017, entry version 22.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase {ECO:0000256|HAMAP-Rule:MF_00727};
DE            EC=2.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00727};
DE   AltName: Full=Transglutaminase {ECO:0000256|HAMAP-Rule:MF_00727};
DE            Short=TGase {ECO:0000256|HAMAP-Rule:MF_00727};
GN   Name=tgl {ECO:0000256|HAMAP-Rule:MF_00727,
GN   ECO:0000313|EMBL:AFQ19316.1};
GN   ORFNames=BTG_29615 {ECO:0000313|EMBL:AFQ19316.1};
OS   Bacillus thuringiensis HD-771.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1218175 {ECO:0000313|EMBL:AFQ19316.1, ECO:0000313|Proteomes:UP000005259};
RN   [1] {ECO:0000313|EMBL:AFQ19316.1, ECO:0000313|Proteomes:UP000005259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HD-771 {ECO:0000313|EMBL:AFQ19316.1,
RC   ECO:0000313|Proteomes:UP000005259};
RA   Doggett N., Teshima H., Bruce D., Detter J.C., Johnson S.L., Han C.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably plays a role in the assembly of the spore coat
CC       proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links.
CC       {ECO:0000256|HAMAP-Rule:MF_00727}.
CC   -!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3). {ECO:0000256|HAMAP-Rule:MF_00727}.
CC   -!- SIMILARITY: Belongs to the bacillus TGase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00727}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP003752; AFQ19316.1; -; Genomic_DNA.
DR   RefSeq; WP_000635353.1; NC_018500.1.
DR   EnsemblBacteria; AFQ19316; AFQ19316; BTG_29615.
DR   KEGG; bti:BTG_29615; -.
DR   PATRIC; fig|1218175.3.peg.5956; -.
DR   KO; K00686; -.
DR   Proteomes; UP000005259; Chromosome.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00727; Tgl; 1.
DR   InterPro; IPR020916; Gln_gamma-glutamylTfrase_bac.
DR   ProDom; PD119415; PD119415; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:AFQ19316.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005259};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:AFQ19316.1}.
SQ   SEQUENCE   276 AA;  31578 MW;  A490D858F1C47794 CRC64;
     MIVIGRSIVH PYITNEYEPF VAEKQQILSI MAGNQEVYSF RTADELSFDL NLRVNIIISA
     LELFQSGFQF RTFQQSFCNP QYWKRTSLGG FELLPNIPPS IAIQDIFKNG KLYGTECATA
     MIIIFYKALL SLYEEETFNR LFANLLLYTW DYDQDLRLIT KTGGDLVPGD LVYFKNPQVN
     PSTIEWQGEN TIYLGNFFFY GHGVGVKTKE EIIYSLNERR VPYAFISAFL TDTITRIDSR
     IMSQYASSST PQTSISFIPI RDDAIVATVG HTTTIY
//
DBGET integrated database retrieval system