ID   TGL_BACC3               Reviewed;         276 AA.
AC   C1EPX7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
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}; OrderedLocusNames=BCA_4068;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001407; ACO30346.1; -; Genomic_DNA.
DR   RefSeq; WP_000635324.1; NZ_CP009318.1.
DR   AlphaFoldDB; C1EPX7; -.
DR   SMR; C1EPX7; -.
DR   EnsemblBacteria; ACO30346; ACO30346; BCA_4068.
DR   KEGG; bcx:BCA_4068; -.
DR   PATRIC; fig|572264.18.peg.4020; -.
DR   OMA; FYAFECA; -.
DR   Proteomes; UP000002210; 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_1000197962"
SQ   SEQUENCE   276 AA;  31460 MW;  889EA7E81E3D8B9D CRC64;
     MIVIGRSIVH PYITNEYEPF AAEKQQILSI MAGNQEIYSF RTSDELSFDL NLRVNIITSA
     LELFQSGFQF RTFQQSFCNP QYWKRTSLGG FELLPNIPPS IAIQDIFKNG KLYGTECATA
     MIIIFYKALL SLYEEETFNR LFANLLLYTW DYDQDLKLIT KTGGDLVPGD LVYFKNPQVN
     PATIEWQGEN TIYLGNFFFY GHGVGVKTKE EIIYALNERR VPYAFISAFL TDTITRIDSR
     LMSYHASPST PQTSIGFIPI RDDAIVATVG NTTTVY