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Database: UniProt/TrEMBL
Entry: A0A0H4NYH2_9BACI
LinkDB: A0A0H4NYH2_9BACI
Original site: A0A0H4NYH2_9BACI 
ID   A0A0H4NYH2_9BACI        Unreviewed;       270 AA.
AC   A0A0H4NYH2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-SEP-2017, entry version 9.
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=BSM4216_1313 {ECO:0000313|EMBL:AKP46594.1};
OS   Bacillus smithii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP46594.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP46594.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP46594.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B.,
RA   Vriesendorp B., van de Weijer A.H.P., Schaap P.J., de Vos W.M.,
RA   van der Oost J., van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain
RT   DSM 4216T.";
RL   Submitted (JUL-2015) 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; CP012024; AKP46594.1; -; Genomic_DNA.
DR   RefSeq; WP_048623009.1; NZ_CP012024.1.
DR   EnsemblBacteria; AKP46594; AKP46594; BSM4216_1313.
DR   KEGG; bsm:BSM4216_1313; -.
DR   KO; K00686; -.
DR   Proteomes; UP000036353; 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:AKP46594.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036353};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036353};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:AKP46594.1}.
SQ   SEQUENCE   270 AA;  31587 MW;  5858EB36A83D8488 CRC64;
     MIIINQKLED FSQMDLGTLS NEASTILQLM GKYSTVYEYE TKEQLEFELA IRLQIIQAAK
     RLYKSGVHFA TFSTSKCNEK YWTLTEKGAF ALKTNVLPQT AIEDIFRNGR KYAFECATAM
     VIVFYKAVLE IIDKEQFNLL FSNLYLYDWQ YDQDLDLRSH KGTDFLPGDC VYFINPDHDP
     NTPEWQGENA IVLDERLYYA HGIGITTRQR IIDILNTKRK QNPNQSAFLT NQITRLNFRS
     LLPYKPKVNR DHHHVHQHSS LFSDDVNYFV
//
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