TGL_BACAH
ID TGL_BACAH Reviewed; 276 AA.
AC A0RHX9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=BALH_3589;
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam;
RX PubMed=17337577; DOI=10.1128/jb.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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; CP000485; ABK86822.1; -; Genomic_DNA.
DR RefSeq; WP_000635324.1; NC_008600.1.
DR AlphaFoldDB; A0RHX9; -.
DR SMR; A0RHX9; -.
DR EnsemblBacteria; ABK86822; ABK86822; BALH_3589.
DR KEGG; btl:BALH_3589; -.
DR HOGENOM; CLU_088922_0_0_9; -.
DR OMA; FYAFECA; -.
DR Proteomes; UP000000761; 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_1000045887"
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