ID   TGL_BACC4               Reviewed;         276 AA.
AC   B7H6V0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase {ECO:0000255|HAMAP-Rule:MF_00727};
DE            EC=2.3.2.13 {ECO:0000255|HAMAP-Rule:MF_00727};
DE   AltName: Full=Transglutaminase {ECO:0000255|HAMAP-Rule:MF_00727};
DE            Short=TGase {ECO:0000255|HAMAP-Rule:MF_00727};
GN   Name=tgl {ECO:0000255|HAMAP-Rule:MF_00727};
GN   OrderedLocusNames=BCB4264_A4066;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) 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:0000255|HAMAP-Rule:MF_00727}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC         lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00727};
CC   -!- SIMILARITY: Belongs to the bacillus TGase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00727}.
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DR   EMBL; CP001176; ACK62256.1; -; Genomic_DNA.
DR   RefSeq; WP_000635337.1; NZ_VEHB01000002.1.
DR   AlphaFoldDB; B7H6V0; -.
DR   SMR; B7H6V0; -.
DR   EnsemblBacteria; ACK62256; ACK62256; BCB4264_A4066.
DR   GeneID; 67508597; -.
DR   KEGG; bcb:BCB4264_A4066; -.
DR   HOGENOM; CLU_088922_0_0_9; -.
DR   OMA; FYAFECA; -.
DR   Proteomes; UP000007096; 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   Pfam; PF20085; TGL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Sporulation; Transferase.
FT   CHAIN           1..276
FT                   /note="Protein-glutamine gamma-glutamyltransferase"
FT                   /id="PRO_1000197965"
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