ID   TGL_BACCN               Reviewed;         276 AA.
AC   A7GRZ1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Bcer98_2665;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS22899.1; -; Genomic_DNA.
DR   RefSeq; WP_012095121.1; NC_009674.1.
DR   AlphaFoldDB; A7GRZ1; -.
DR   SMR; A7GRZ1; -.
DR   STRING; 315749.Bcer98_2665; -.
DR   EnsemblBacteria; ABS22899; ABS22899; Bcer98_2665.
DR   KEGG; bcy:Bcer98_2665; -.
DR   eggNOG; ENOG502Z8C5; Bacteria.
DR   HOGENOM; CLU_088922_0_0_9; -.
DR   OMA; FYAFECA; -.
DR   OrthoDB; 1166294at2; -.
DR   Proteomes; UP000002300; 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_1000197968"
SQ   SEQUENCE   276 AA;  31542 MW;  23BCFAD45BA9C0C0 CRC64;
     MIVIGRSIVH PYIMNENEPF AAEKQQFLSI MTGNQEVYSF RTAAELSFDL NVRMHIITSA
     LELFQSGFQF RTFVTSFCNE EYWQRTALGG FQLRPGVSSS IAIRDIFKNG KMYGTECATA
     MIIIFYKALL ELYDEEMFNH LFANLLLYTW DYDRDLKLIT KTAGDIVPGD LVYFKNPQVN
     PASIEWQGEN AIYLGNSFYY GHGVGVKTKE QIIYLLNDRR IPSAFISAYL TDFITRIDSR
     IMSQYASHTP PQTSLGFIPI RDDAIVATIG HTTTIY