GenomeNet

Database: UniProt/TrEMBL
Entry: V5MH78_BACTU
LinkDB: V5MH78_BACTU
Original site: V5MH78_BACTU 
ID   V5MH78_BACTU            Unreviewed;       276 AA.
AC   V5MH78;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-SEP-2017, entry version 15.
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:AHA73523.1};
GN   ORFNames=YBT1518_21985 {ECO:0000313|EMBL:AHA73523.1};
OS   Bacillus thuringiensis YBT-1518.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=529122 {ECO:0000313|EMBL:AHA73523.1, ECO:0000313|Proteomes:UP000018566};
RN   [1] {ECO:0000313|EMBL:AHA73523.1, ECO:0000313|Proteomes:UP000018566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBT-1518 {ECO:0000313|EMBL:AHA73523.1,
RC   ECO:0000313|Proteomes:UP000018566};
RA   Wang P., Zhang C., Guo M., Guo S., Zhu Y., Zheng J., Zhu L., Ruan L.,
RA   Peng D., Sun M.;
RT   "Complete genome sequence of Bacillus thuringiensis YBT-1518, a
RT   typical strain with high toxicity to nematode.";
RL   Submitted (MAY-2013) 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; CP005935; AHA73523.1; -; Genomic_DNA.
DR   RefSeq; WP_000635337.1; NC_022873.1.
DR   SMR; V5MH78; -.
DR   EnsemblBacteria; AHA73523; AHA73523; YBT1518_21985.
DR   KEGG; bthu:YBT1518_21985; -.
DR   PATRIC; fig|529122.4.peg.4393; -.
DR   KO; K00686; -.
DR   Proteomes; UP000018566; 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:AHA73523.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018566};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:AHA73523.1}.
SQ   SEQUENCE   276 AA;  31547 MW;  80274DEB9912BFCE CRC64;
     MIVIGRSIVH PYITNEYEPF AAEKQQILSI MAGNQEVYSF RTADELSFDL NLRVNIIISA
     LELFQSGFQF RTFQQSFCNP QYWKRTSLGG FELLPNIPPS IAIQDIFKNG KLYGTECATA
     MIIIFYKALL SLYEEETFNR LFANLLLYTW DYDQDLRLIT KNGGDLVPGD LVYFKNPQVN
     PATIEWQGEN TIYLGNFFFY GHGVGVKTKE EIIYSLNERR VPYAFISAFL TDTITRIDSR
     IMSQYASSST PQTSISFIPI RDDAIVATVG HTTTIY
//
DBGET integrated database retrieval system