ID   M1PPP9_BACTU            Unreviewed;       276 AA.
AC   M1PPP9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ORFNames=H175_ch4031 {ECO:0000313|EMBL:AGG02743.1};
OS   Bacillus thuringiensis serovar thuringiensis str. IS5056.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1286404 {ECO:0000313|EMBL:AGG02743.1, ECO:0000313|Proteomes:UP000011719};
RN   [1] {ECO:0000313|EMBL:AGG02743.1, ECO:0000313|Proteomes:UP000011719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS5056 {ECO:0000313|EMBL:AGG02743.1};
RX   PubMed=23516221;
RA   Murawska E., Fiedoruk K., Bideshi D.K., Swiecicka I.;
RT   "Complete genome sequence of Bacillus thuringiensis subsp. thuringiensis
RT   strain IS5056, an isolate highly toxic to Trichoplusia ni.";
RL   Genome Announc. 1:E0010813-E0010813(2013).
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:
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:0000256|HAMAP-
CC         Rule:MF_00727};
CC   -!- SIMILARITY: Belongs to the bacillus TGase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00727}.
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DR   EMBL; CP004123; AGG02743.1; -; Genomic_DNA.
DR   RefSeq; WP_000635339.1; NC_020376.1.
DR   AlphaFoldDB; M1PPP9; -.
DR   SMR; M1PPP9; -.
DR   GeneID; 67468275; -.
DR   KEGG; btht:H175_ch4031; -.
DR   PATRIC; fig|1286404.3.peg.4061; -.
DR   HOGENOM; CLU_088922_0_0_9; -.
DR   Proteomes; UP000011719; 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 {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:AGG02743.1};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727, ECO:0000313|EMBL:AGG02743.1}.
SQ   SEQUENCE   276 AA;  31534 MW;  6A27462C94A464A3 CRC64;
     MIVIGRSIVH PYITNEYEPF AAEKQQILSI MAGNQEVYSF RTADELSFDL NLRVNIIISA
     LELFQSGFQF RTFQQSFCNP QYWKRTSLGG FELLPNIPPS IAIQDIFKNG KLYGTECATA
     MIIIFYKALL SLYEEETFNR LFANLLLYTW DYDQDLRLIT KTGGDLVPGD LVYFKNPQVN
     PATIEWQGEN TIYLGNFFFY GHGVGVKTKE EIIYSLNERR VPYAFISAFL TDTITRIDSR
     IMSQYASSST PQTSISFIPI RDDAIVATVG HTTTIY
//