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 27-MAR-2024, entry version 72.
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; Bacillota; 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 KEGG; bpu:BPUM_2792; -.
DR eggNOG; ENOG502Z8C5; Bacteria.
DR HOGENOM; CLU_088922_0_0_9; -.
DR OrthoDB; 1845399at2; -.
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; 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
//
