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Database: UniProt/TrEMBL
Entry: A0A1S6ZDN8_9BACI
LinkDB: A0A1S6ZDN8_9BACI
Original site: A0A1S6ZDN8_9BACI 
ID   A0A1S6ZDN8_9BACI        Unreviewed;       273 AA.
AC   A0A1S6ZDN8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
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   ORFNames=BC359_16015 {ECO:0000313|EMBL:AQX55663.1};
OS   Bacillus flexus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86664 {ECO:0000313|EMBL:AQX55663.1, ECO:0000313|Proteomes:UP000190623};
RN   [1] {ECO:0000313|EMBL:AQX55663.1, ECO:0000313|Proteomes:UP000190623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLBMP 4941 {ECO:0000313|EMBL:AQX55663.1,
RC   ECO:0000313|Proteomes:UP000190623};
RA   Qin S.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   bacteria and their functional gene analysis.";
RL   Submitted (JUL-2016) 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: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; CP016790; AQX55663.1; -; Genomic_DNA.
DR   KEGG; bfx:BC359_16015; -.
DR   KO; K00686; -.
DR   Proteomes; UP000190623; 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:UP000190623};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:AQX55663.1}.
SQ   SEQUENCE   273 AA;  31452 MW;  1723480E1A28F592 CRC64;
     MIIVQGRALN MNAVPYSMLE ANKAQILRKM AQYQTIYRYD NIMQLDFELT TRLRIVEASY
     LLYRSGARFA TFKESECNET YWLRTEKGGF KLKENVLPSV ALNDIFFNGS LYAFECAVAI
     VMVFYRGVLE SIGERDFNQL FTNLVLYSGK FDEDLNLQNH HGYDFLEGDC AYFKNPDHHE
     DTPQWQGENT IIVGDDLYFG HGVGVKSAEG IIELLNEKRK ENATESAYLT SYITRVGFRY
     LSQFYVHRDV LVEVDYDKLP LVVSQIGSST YIG
//
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