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Database: UniProt/TrEMBL
Entry: F0PSS2_BACT0
LinkDB: F0PSS2_BACT0
Original site: F0PSS2_BACT0 
ID   F0PSS2_BACT0            Unreviewed;       276 AA.
AC   F0PSS2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-SEP-2017, entry version 29.
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:ADY23123.1};
GN   OrderedLocusNames=YBT020_19475 {ECO:0000313|EMBL:ADY23123.1};
OS   Bacillus thuringiensis subsp. finitimus (strain YBT-020).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=930170 {ECO:0000313|EMBL:ADY23123.1, ECO:0000313|Proteomes:UP000007483};
RN   [1] {ECO:0000313|EMBL:ADY23123.1, ECO:0000313|Proteomes:UP000007483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBT-020 {ECO:0000313|EMBL:ADY23123.1,
RC   ECO:0000313|Proteomes:UP000007483};
RX   PubMed=21398543; DOI=10.1128/JB.00267-11;
RA   Zhu Y., Shang H., Zhu Q., Ji F., Wang P., Fu J., Deng Y., Xu C.,
RA   Ye W., Zheng J., Zhu L., Ruan L., Peng D., Sun M.;
RT   "Complete genome sequence of Bacillus thuringiensis serovar finitimus
RT   strain YBT-020.";
RL   J. Bacteriol. 193:2379-2380(2011).
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; CP002508; ADY23123.1; -; Genomic_DNA.
DR   RefSeq; WP_000635349.1; NC_017200.1.
DR   EnsemblBacteria; ADY23123; ADY23123; YBT020_19475.
DR   KEGG; btf:YBT020_19475; -.
DR   PATRIC; fig|930170.3.peg.3870; -.
DR   KO; K00686; -.
DR   OMA; GALELKY; -.
DR   OrthoDB; POG091H0WEC; -.
DR   Proteomes; UP000007483; 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   ECO:0000313|EMBL:ADY23123.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007483};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:ADY23123.1}.
SQ   SEQUENCE   276 AA;  31489 MW;  C845D28B1FE6F8F0 CRC64;
     MIVIGRSIVH PYITNEYEPF ANEKQQILSI MAGNQEIYSF RTSDELSFDL NLRVNIITSA
     LELFQSGFQF RTFQQSFCNP QYWKRTSLGG FELLPNIPPS IAIQDIFKNG KLYGTECATA
     MIIIFYKALL SLYDEETFNR LFANLLLYTW DYDQDLKLIT KTGGDLVPGD LVYFKNPQVN
     PATIEWQGEN TIYLGNFFFY GHGVGVKTKE EIIYALNERR VPYAFISAFL TDTITRIDSR
     LMSYHASPST PQTSIGFIPI RDDAIVATVG NTTTVY
//
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