TGL_BACAA
ID TGL_BACAA Reviewed; 276 AA.
AC C3P6X0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=BAA_4198;
OS Bacillus anthracis (strain A0248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=592021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A0248;
RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA Brettin T.;
RT "Genome sequence of Bacillus anthracis A0248.";
RL Submitted (APR-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}.
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DR EMBL; CP001598; ACQ48242.1; -; Genomic_DNA.
DR RefSeq; WP_000635329.1; NC_012659.1.
DR AlphaFoldDB; C3P6X0; -.
DR SMR; C3P6X0; -.
DR GeneID; 45023850; -.
DR KEGG; bai:BAA_4198; -.
DR HOGENOM; CLU_088922_0_0_9; -.
DR OMA; FYAFECA; -.
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_1000197960"
SQ SEQUENCE 276 AA; 31459 MW; 783EA7E21E9A3D30 CRC64;
MIVIGRSIVH PYITNEYEPF AAEKQQILSI MAGNQEIYSF RTSDELSFDL NLRVNIITSA
LELFQSGFQF RTFQQSFCNP QYWKRTSLGG FELLPNIPPS IAIQDIFKNG KLYGTECATA
MIIIFYKALL SLYEKETFNR LFANLLLYTW DYDQDLKLIT KTGGDLVPGD LVYFKNPQVN
PATIEWQGEN TIYLGNFFFY GHGVGVKTKE EIIYALNERR VPYAFISAFL TDTITRIDSR
LMSYHASPST PQTSIGFIPI RDDAIVATVG NTTTVY