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Database: UniProt/SWISS-PROT
Entry: TGL_BACHK
LinkDB: TGL_BACHK
Original site: TGL_BACHK 
ID   TGL_BACHK               Reviewed;         276 AA.
AC   Q6HEJ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   07-JUN-2017, entry version 59.
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=BT9727_3708;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   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., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3). {ECO:0000255|HAMAP-Rule:MF_00727}.
CC   -!- SIMILARITY: Belongs to the bacillus TGase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00727}.
DR   EMBL; AE017355; AAT63084.1; -; Genomic_DNA.
DR   RefSeq; WP_000635329.1; NC_005957.1.
DR   RefSeq; YP_038027.1; NC_005957.1.
DR   SMR; Q6HEJ9; -.
DR   EnsemblBacteria; AAT63084; AAT63084; BT9727_3708.
DR   GeneID; 2855089; -.
DR   KEGG; btk:BT9727_3708; -.
DR   PATRIC; fig|281309.8.peg.3946; -.
DR   HOGENOM; HOG000262157; -.
DR   KO; K00686; -.
DR   OMA; GALELKY; -.
DR   Proteomes; UP000001301; Chromosome.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   HAMAP; MF_00727; Tgl; 1.
DR   InterPro; IPR020916; Gln_gamma-glutamylTfrase_bac.
DR   ProDom; PD119415; PD119415; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Complete proteome; Sporulation; Transferase.
FT   CHAIN         1    276       Protein-glutamine gamma-
FT                                glutamyltransferase.
FT                                /FTId=PRO_1000045889.
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
//
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