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Database: UniProt/TrEMBL
Entry: K0FRZ0_BACTU
LinkDB: K0FRZ0_BACTU
Original site: K0FRZ0_BACTU 
ID   K0FRZ0_BACTU            Unreviewed;       276 AA.
AC   K0FRZ0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-SEP-2017, entry version 21.
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   ECO:0000313|EMBL:AFU14671.1};
GN   ORFNames=MC28_3249 {ECO:0000313|EMBL:AFU14671.1};
OS   Bacillus thuringiensis MC28.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1195464 {ECO:0000313|EMBL:AFU14671.1, ECO:0000313|Proteomes:UP000006284};
RN   [1] {ECO:0000313|EMBL:AFU14671.1, ECO:0000313|Proteomes:UP000006284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC28 {ECO:0000313|EMBL:AFU14671.1};
RX   PubMed=23209229; DOI=10.1128/JB.01861-12;
RA   Guan P., Ai P., Dai X., Zhang J., Xu L., Zhu J., Li Q., Deng Q.,
RA   Li S., Wang S., Liu H., Wang L., Li P., Zheng A.;
RT   "Complete Genome Sequence of Bacillus thuringiensis Serovar Sichuansis
RT   Strain MC28.";
RL   J. Bacteriol. 194:6975-6975(2012).
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: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3). {ECO:0000256|HAMAP-Rule:MF_00727}.
CC   -!- SIMILARITY: Belongs to the bacillus TGase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00727}.
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DR   EMBL; CP003687; AFU14671.1; -; Genomic_DNA.
DR   RefSeq; WP_000635336.1; NC_018693.1.
DR   EnsemblBacteria; AFU14671; AFU14671; MC28_3249.
DR   KEGG; btm:MC28_3249; -.
DR   PATRIC; fig|1195464.3.peg.3308; -.
DR   KO; K00686; -.
DR   OrthoDB; POG091H0WEC; -.
DR   Proteomes; UP000006284; 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   ProDom; PD119415; PD119415; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006284};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:AFU14671.1}.
SQ   SEQUENCE   276 AA;  31480 MW;  F2F2E6CC0F65209D CRC64;
     MIVIGRSIVH PYITNEYEPF AAEKQQILSI MAGNQEVYSF RTADELSFDL NLRVNIIISA
     LELFQSGFQF RTFQQSFCNP QFWKRTSLGG FQLLPNIPPS IAIQDIFKNG KLYGTECATA
     MIIIFYKALL SLYEEETFNR LFANLLLYTW DYDQDLKLIT KTGGDLVPGD LVYFKNPQVN
     PATIEWQGEN TIYLGNFFFY GHGVGVKTKE EIIYSLNERR VPYAFISAFL TDTITRIDSR
     IMSQYASPNT PQTAIGFIPI RDDAIVATVG HTTTIY
//
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