ID   D4G0L4_BACNB            Unreviewed;       245 AA.
AC   D4G0L4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 48.
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:BAI86645.1};
GN   ORFNames=BSNT_09584 {ECO:0000313|EMBL:BAI86645.1};
OS   Bacillus subtilis subsp. natto (strain BEST195).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=645657 {ECO:0000313|EMBL:BAI86645.1, ECO:0000313|Proteomes:UP000006805};
RN   [1] {ECO:0000313|EMBL:BAI86645.1, ECO:0000313|Proteomes:UP000006805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEST195 {ECO:0000313|EMBL:BAI86645.1,
RC   ECO:0000313|Proteomes:UP000006805};
RX   PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA   Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA   Itaya M., Sakakibara Y.;
RT   "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT   from very short read data.";
RL   BMC Genomics 11:243-243(2010).
RN   [2] {ECO:0000313|EMBL:BAI86645.1, ECO:0000313|Proteomes:UP000006805}
RP   GENOME REANNOTATION.
RC   STRAIN=BEST195 {ECO:0000313|EMBL:BAI86645.1,
RC   ECO:0000313|Proteomes:UP000006805};
RX   PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA   Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT   "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT   long reads with high-quality short reads.";
RL   PLoS ONE 9:E109999-E109999(2014).
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; AP011541; BAI86645.1; -; Genomic_DNA.
DR   RefSeq; WP_003228904.1; NC_017196.2.
DR   AlphaFoldDB; D4G0L4; -.
DR   SMR; D4G0L4; -.
DR   STRING; 86029.AWV81_16055; -.
DR   KEGG; bso:BSNT_09584; -.
DR   PATRIC; fig|645657.3.peg.4050; -.
DR   HOGENOM; CLU_088922_0_0_9; -.
DR   Proteomes; UP000006805; 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   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727}.
SQ   SEQUENCE   245 AA;  28295 MW;  457BC0836B119AC6 CRC64;
     MIIVSGQLLR PQDIENWQID QNLNPLLKEM IETPVQFDYH SIAELMFELK LRMNIVAAAK
     TLHKSGAKFA TFLKTYGNTT YWRVSPEGAL ELKYRMPPSK AIRDIAENGP FYAFECATAI
     VIIYYLALID TIGEDKFNAS FDRIILYDWH YEKLPIYTET GHHFFLGDCL YFKNPEFDPQ
     KAQWRGENVI LLGEDKYFAH GLGILNGKQI IDKLNSFRKK GALQSAYLLS QATRLDVPSL
     FRIVR
//