TGL_BACC7
ID TGL_BACC7 Reviewed; 276 AA.
AC B7HME8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=BCAH187_A4082;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
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; CP001177; ACJ78754.1; -; Genomic_DNA.
DR RefSeq; WP_000635351.1; NC_011658.1.
DR AlphaFoldDB; B7HME8; -.
DR SMR; B7HME8; -.
DR EnsemblBacteria; ACJ78754; ACJ78754; BCAH187_A4082.
DR GeneID; 64199304; -.
DR KEGG; bcr:BCAH187_A4082; -.
DR HOGENOM; CLU_088922_0_0_9; -.
DR OMA; FYAFECA; -.
DR OrthoDB; 1166294at2; -.
DR Proteomes; UP000002214; 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_1000197963"
SQ SEQUENCE 276 AA; 31429 MW; F4E766295880FDA7 CRC64;
MIVIGRSIVH PYITNEYEPF ANEKQQILSI MAGNQEIYSF RTSGELSFDL NLRVNIITSA
LELFQSGFQF RTFQQSFCNP QYWKRTSLGG FELLPNIPPS IAIQDIFKNG KLYGTECATA
MIIIFYKALL ALYEEETFNR LFANLLLYTW DYDQDLKLIT KTGGDLVPGD LVYFKNPQVN
PATIEWQGEN TIYLGNFFFY GHGVGVKTKE EIIYALNERR VPYAFISAFL TDTITRIDSR
LMSYHASPST PQTSIGFIPI RDDAIVATVG NTTTVY