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Database: UniProt/TrEMBL
Entry: D5DEI8_BACMD
LinkDB: D5DEI8_BACMD
Original site: D5DEI8_BACMD 
ID   D5DEI8_BACMD            Unreviewed;       271 AA.
AC   D5DEI8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-SEP-2017, entry version 38.
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   OrderedLocusNames=BMD_2424 {ECO:0000313|EMBL:ADF39270.1};
OS   Bacillus megaterium (strain DSM 319).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF39270.1, ECO:0000313|Proteomes:UP000002365};
RN   [1] {ECO:0000313|Proteomes:UP000002365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 319 {ECO:0000313|Proteomes:UP000002365};
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J.,
RA   Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J.,
RA   Vary P.S.;
RT   "Genome sequences of the industrial vitamin B12-producers B.
RT   megaterium QM B1551 and DSM319 reveal new insights into the Bacillus
RT   genome evolution and pan-genome structure.";
RL   Submitted (FEB-2010) 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; CP001982; ADF39270.1; -; Genomic_DNA.
DR   RefSeq; WP_013083260.1; NC_014103.1.
DR   EnsemblBacteria; ADF39270; ADF39270; BMD_2424.
DR   KEGG; bmd:BMD_2424; -.
DR   PATRIC; fig|592022.4.peg.2377; -.
DR   HOGENOM; HOG000262157; -.
DR   KO; K00686; -.
DR   OMA; GALELKY; -.
DR   OrthoDB; POG091H0WEC; -.
DR   Proteomes; UP000002365; 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:ADF39270.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002365};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:ADF39270.1}.
SQ   SEQUENCE   271 AA;  31281 MW;  042F94E07450229C CRC64;
     MIKVNQQIVK ISDLNNSSLT KEKADILKQM DAYREVYEYA TFDQLDFDVS VKLQIIESSV
     LLRKSGAKFA TFARSRCNEK YWKRTDNGGF QLLPTVSPHQ AIDDIFYNGH EYAFECATAV
     IIIFYKAVLN NIGKANFNRL FADLYLHDWQ YDEDLELHGY KGSDYLPGDC AYFKNPDYNP
     DTPQWKGENT IVLDETLYFG HGIGITTRER IIEVLNLKRK DDAKQSAYLS DEIVRLHTAH
     LSYFAVRYEP VVWYDRNSAI ISTIGSITYV A
//
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