ID   TGL_HALH5               Reviewed;         284 AA.
AC   Q9K5W7;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=BH3970;
OS   Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Halalkalibacterium (ex Joshi et al. 2022).
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB07689.1; -; Genomic_DNA.
DR   PIR; B84146; B84146.
DR   AlphaFoldDB; Q9K5W7; -.
DR   SMR; Q9K5W7; -.
DR   STRING; 272558.gene:10729883; -.
DR   KEGG; bha:BH3970; -.
DR   eggNOG; ENOG502Z8C5; Bacteria.
DR   HOGENOM; CLU_088922_0_0_9; -.
DR   OrthoDB; 1845399at2; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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..284
FT                   /note="Protein-glutamine gamma-glutamyltransferase"
FT                   /id="PRO_0000213724"
SQ   SEQUENCE   284 AA;  32578 MW;  5A5A855E9B064F35 CRC64;
     MGNDMIQVAG RPFSLESTTD FGRVERAILQ QMLDSSEWFS YSSMNELRFE LNVRINIMES
     AKEMNASQVT FTIFEHASCN PEYWTLTSTG GFLVRSDVRP SDAILDIYRN GTLYGFECAT
     AIIIIYYQAI LKSIGQLRFD SIFQHLYLYS WHTHPGLELH TFHADRFLPG DVVYFNNPDF
     HPDTPWFRGE NAVVLSDGTF FGHGFGIMTA EQMIQSLNSY RFPGSMQPAY LANLITRISP
     LTIRNLLTLQ SDRTTYHYSK AVIHHNLCSI SSMDYQYYLL SLNG
//