ID   I2C9F8_BACAY            Unreviewed;       245 AA.
AC   I2C9F8;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:AFJ63282.1};
GN   ORFNames=MUS_3406 {ECO:0000313|EMBL:AFJ63282.1};
OS   Bacillus amyloliquefaciens (strain Y2) (Bacillus amyloliquefaciens subsp.
OS   plantarum (strain B9601-Y2)).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1155777 {ECO:0000313|EMBL:AFJ63282.1, ECO:0000313|Proteomes:UP000002878};
RN   [1] {ECO:0000313|EMBL:AFJ63282.1, ECO:0000313|Proteomes:UP000002878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y2 {ECO:0000313|EMBL:AFJ63282.1};
RX   PubMed=23357245; DOI=10.1016/j.jbiotec.2012.12.014;
RA   He P., Hao K., Blom J., Ruckert C., Vater J., Mao Z., Wu Y., Hou M., He P.,
RA   He Y., Borriss R.;
RT   "Genome sequence of the plant growth promoting strain Bacillus
RT   amyloliquefaciens subsp. plantarum B9601-Y2 and expression of mersacidin
RT   and other secondary metabolites.";
RL   J. Biotechnol. 164:281-291(2012).
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; CP003332; AFJ63282.1; -; Genomic_DNA.
DR   RefSeq; WP_014418735.1; NC_017912.1.
DR   AlphaFoldDB; I2C9F8; -.
DR   GeneID; 66323139; -.
DR   KEGG; bqy:MUS_3406; -.
DR   KEGG; bya:BANAU_3020; -.
DR   PATRIC; fig|1126211.3.peg.3240; -.
DR   HOGENOM; CLU_088922_0_0_9; -.
DR   Proteomes; UP000002878; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:AFJ63282.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00727, ECO:0000313|EMBL:AFJ63282.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   245 AA;  28298 MW;  45FDD92A7B3FEA59 CRC64;
     MIIISGQVLR PQDIANWQTE ENLVPYINEL LNSPVQFDYG SIAELMFEVR LRRHIVEAAR
     ELHGSGVKFA TFAKTYGNTA YWRVTPEGAL ELKYRIPASK AIRDIIENGA FYAFECATAI
     VVIYYLAVLK TMGEERFNRR FRDITLYDWH YEHLPIYTET GSHFLRGDCL YFKNPDFNPA
     KAQWRGENVI VMGNDQYFAH GLGILTAEQI IQRLNSLRKK NAVQPAYLLN QATRLDAPAL
     YQIMH
//