ID   N0ASC6_9BACI            Unreviewed;       283 AA.
AC   N0ASC6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
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:AGK53588.1};
GN   ORFNames=B1NLA3E_09130 {ECO:0000313|EMBL:AGK53588.1};
OS   Bacillus sp. 1NLA3E.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK53588.1, ECO:0000313|Proteomes:UP000013300};
RN   [1] {ECO:0000313|EMBL:AGK53588.1, ECO:0000313|Proteomes:UP000013300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1NLA3E {ECO:0000313|EMBL:AGK53588.1};
RX   PubMed=23833140;
RA   Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA   Brooks S., Kostka J.E., Green S.J.;
RT   "Genome sequences for three denitrifying bacterial strains isolated from a
RT   uranium- and nitrate-contaminated subsurface environment.";
RL   Genome Announc. 1:e00449-13(2013).
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:
CC       Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC         lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00727};
CC   -!- SIMILARITY: Belongs to the bacillus TGase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00727}.
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DR   EMBL; CP005586; AGK53588.1; -; Genomic_DNA.
DR   RefSeq; WP_015593647.1; NC_021171.1.
DR   AlphaFoldDB; N0ASC6; -.
DR   STRING; 666686.B1NLA3E_09130; -.
DR   KEGG; baci:B1NLA3E_09130; -.
DR   eggNOG; ENOG502Z8C5; Bacteria.
DR   HOGENOM; CLU_088922_0_0_9; -.
DR   OrthoDB; 1845399at2; -.
DR   Proteomes; UP000013300; 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   Pfam; PF20085; TGL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00727,
KW   ECO:0000313|EMBL:AGK53588.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013300};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727, ECO:0000313|EMBL:AGK53588.1}.
SQ   SEQUENCE   283 AA;  32941 MW;  B1E75E55DCDFA7CE CRC64;
     MIQLSGIPFQ QSGMWPPGYI ESVIILKMHE APAVYSYQSM DELLFELKLR KKIIESARSM
     SRGHARFASF AKSRCNPRFW HLTNTGGFWL RYDVKPSDAI RDIYKNSSLY AFECATAKVI
     IYYDAILNSI DEHLFNQLFQ NLYLYSWHFD PDFGIHSFYS DHLIPGDVAY FNNPDFNPKT
     PWWKGENAVV LGDGKYFGHG LGIRNAEQMI QALNKRRKPG SNQSAYLTNI VTSLSFKQLT
     NFLMLQQRFS DYKIKHAVIH HNESSISFAR YLFYLNKVNN RIT
//