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Database: UniProt/TrEMBL
Entry: A0A0B6ALY7_BACMB
LinkDB: A0A0B6ALY7_BACMB
Original site: A0A0B6ALY7_BACMB 
ID   A0A0B6ALY7_BACMB        Unreviewed;       271 AA.
AC   A0A0B6ALY7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-SEP-2017, entry version 12.
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=BG04_4823 {ECO:0000313|EMBL:AJI22087.1};
OS   Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC
OS   15308 / NCIMB 9376 / NCTC 10342 / VKM B-512).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1348623 {ECO:0000313|EMBL:AJI22087.1, ECO:0000313|Proteomes:UP000031829};
RN   [1] {ECO:0000313|EMBL:AJI22087.1, ECO:0000313|Proteomes:UP000031829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 /
RC   NCTC 10342 / VKM B-512 {ECO:0000313|Proteomes:UP000031829};
RX   PubMed=25931591;
RA   Johnson S.L., Daligault H.E., Davenport K.W., Jaissle J., Frey K.G.,
RA   Ladner J.T., Broomall S.M., Bishop-Lilly K.A., Bruce D.C.,
RA   Gibbons H.S., Coyne S.R., Lo C.C., Meincke L., Munk A.C.,
RA   Koroleva G.I., Rosenzweig C.N., Palacios G.F., Redden C.L.,
RA   Minogue T.D., Chain P.S.;
RT   "Complete genome sequences for 35 biothreat assay-relevant bacillus
RT   species.";
RL   Genome Announc. 3:0-0(2015).
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; CP009920; AJI22087.1; -; Genomic_DNA.
DR   RefSeq; WP_034651922.1; NZ_JJMH01000072.1.
DR   EnsemblBacteria; AJI22087; AJI22087; BG04_4823.
DR   GeneID; 29908891; -.
DR   KEGG; bmeg:BG04_4823; -.
DR   KO; K00686; -.
DR   Proteomes; UP000031829; 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:UP000031829};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727}.
SQ   SEQUENCE   271 AA;  31290 MW;  04283869745DA86C CRC64;
     MIKVNHQIVK 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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