ID   TGL_BACP2               Reviewed;         246 AA.
AC   A8FGT0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase {ECO:0000255|HAMAP-Rule:MF_00727};
DE            EC=2.3.2.13 {ECO:0000255|HAMAP-Rule:MF_00727};
DE   AltName: Full=Transglutaminase {ECO:0000255|HAMAP-Rule:MF_00727};
DE            Short=TGase {ECO:0000255|HAMAP-Rule:MF_00727};
GN   Name=tgl {ECO:0000255|HAMAP-Rule:MF_00727}; OrderedLocusNames=BPUM_2792;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00727};
CC   -!- SIMILARITY: Belongs to the bacillus TGase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00727}.
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DR   EMBL; CP000813; ABV63447.1; -; Genomic_DNA.
DR   RefSeq; WP_012011070.1; NZ_VEIS01000026.1.
DR   AlphaFoldDB; A8FGT0; -.
DR   SMR; A8FGT0; -.
DR   STRING; 315750.BPUM_2792; -.
DR   EnsemblBacteria; ABV63447; ABV63447; BPUM_2792.
DR   KEGG; bpu:BPUM_2792; -.
DR   eggNOG; ENOG502Z8C5; Bacteria.
DR   HOGENOM; CLU_088922_0_0_9; -.
DR   OMA; FYAFECA; -.
DR   OrthoDB; 1166294at2; -.
DR   Proteomes; UP000001355; 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; Reference proteome; Sporulation; Transferase.
FT   CHAIN           1..246
FT                   /note="Protein-glutamine gamma-glutamyltransferase"
FT                   /id="PRO_1000197970"
SQ   SEQUENCE   246 AA;  28411 MW;  C0A3B05352480B41 CRC64;
     MIILSGQPVT NEQLASFQLE GQKRIILMQL QASNDTFRYR QASDLLFEVT LRSNIMNAAR
     DLNKSGASFA IFQRSRANDA FWRVSEAGAL ELRYQVEPSR GIKDIFENGS QYAFECATAI
     VIVFYMGVLQ TVGDEKFNRR LRSLTLYDWH YDTLSIYTER GNDFIYGDCL YFENPEFSYQ
     QSQWRGENVI YLGEDQYYGH GLGILTAAEI IDKLNKRRRP GAVQSAYLLP QTTRMDVIYL
     RQMFGS