ID TGAS_STRMB Reviewed; 407 AA. AC P81453; N1NTU7; Q8KRJ2; Q9ZAF5; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 07-NOV-2003, sequence version 2. DT 28-JUN-2023, entry version 97. DE RecName: Full=Protein-glutamine gamma-glutamyltransferase; DE EC=2.3.2.13; DE AltName: Full=MTG; DE AltName: Full=Transglutaminase; DE Short=TGase; DE Flags: Precursor; OS Streptomyces mobaraensis (Streptoverticillium mobaraense). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=35621; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 RC / NRRL B-3729 / VKM Ac-928; RX PubMed=12514016; DOI=10.1128/aem.69.1.358-366.2003; RA Kikuchi Y., Date M., Yokoyama K., Umezawa Y., Matsui H.; RT "Secretion of active-form Streptoverticillium mobaraense transglutaminase RT by Corynebacterium glutamicum: processing of the pro-transglutaminase by a RT cosecreted subtilisin-like protease from Streptomyces albogriseolus."; RL Appl. Environ. Microbiol. 69:358-366(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 RC / NRRL B-3729 / VKM Ac-928; RA Zindel S., Froels S., Kletzin A., Pfeifer F., Fuchsbauer H.L.; RT "Confirmation of the genes coding a transglutaminase and a prolyl RT tri/tetrapeptidyl aminopeptidase from Streptomyces mobaraensis."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-407, AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 27441 / CBS 777.72 / DSM 40587 / JCM 4778 / NBRC 13476 / RC VKM Ac-879; RX PubMed=9839945; DOI=10.1046/j.1432-1327.1998.2570570.x; RA Pasternack R., Dorsch S., Otterbach J.T., Robenek I.R., Wolf S., RA Fuchsbauer H.-L.; RT "Bacterial pro-transglutaminase from Streptoverticillium mobaraense: RT purification, characterisation and sequence of the zymogen."; RL Eur. J. Biochem. 257:570-576(1998). RN [4] RP PROTEIN SEQUENCE OF 77-407, AND MASS SPECTROMETRY. RC STRAIN=S-8112; RX PubMed=8099353; DOI=10.1016/s0021-9258(19)50238-1; RA Kanaji T., Ozaki H., Takao T., Kawajiri H., Ide H., Motoki M., RA Shimonishi Y.; RT "Primary structure of microbial transglutaminase from Streptoverticillium RT sp. strain s-8112."; RL J. Biol. Chem. 268:11565-11572(1993). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-407. RC STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 RC / NRRL B-3729 / VKM Ac-928; RX PubMed=12221081; DOI=10.1074/jbc.m203933200; RA Kashiwagi T., Yokoyama K., Ishikawa K., Ono K., Ejima D., Matsui H., RA Suzuki E.; RT "Crystal structure of microbial transglutaminase from Streptoverticillium RT mobaraense."; RL J. Biol. Chem. 277:44252-44260(2002). CC -!- FUNCTION: Catalyzes the cross-linking of proteins and the conjugation CC of polyamines to proteins. 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; CC -!- MASS SPECTROMETRY: Mass=37869.2; Mass_error=8.8; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:8099353}; CC -!- BIOTECHNOLOGY: Sold under the name Activa TG by Ajinomoto. It has the CC ability to cross-link protein molecules present in food without the use CC of salt or binders. Used to improve some of the physical properties CC such as firmness, elasticity and moisture retention of food such as CC meat, poultry and seafood. CC -!- SIMILARITY: Belongs to the bacterial TGase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF531437; AAM95951.1; -; Genomic_DNA. DR EMBL; HF968462; CCW72544.1; -; Genomic_DNA. DR EMBL; Y18315; CAA77128.1; -; Genomic_DNA. DR PDB; 1IU4; X-ray; 2.40 A; A/B/C/D=77-407. DR PDB; 3IU0; X-ray; 1.90 A; A=32-407. DR PDBsum; 1IU4; -. DR PDBsum; 3IU0; -. DR AlphaFoldDB; P81453; -. DR SMR; P81453; -. DR Allergome; 11851; Str mo TrGlu. DR BRENDA; 2.3.2.13; 6129. DR EvolutionaryTrace; P81453; -. DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.1360.10; Protein-glutamine gamma-glutamyltransferase; 1. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR015107; Transglut_prok. DR InterPro; IPR037084; Transglut_prok_sf. DR Pfam; PF09017; Transglut_prok; 1. DR PIRSF; PIRSF037210; Transglut_prok; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Direct protein sequencing; Signal; KW Transferase; Zymogen. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT PROPEP 32..76 FT /evidence="ECO:0000269|PubMed:8099353" FT /id="PRO_0000033656" FT CHAIN 77..407 FT /note="Protein-glutamine gamma-glutamyltransferase" FT /id="PRO_0000033657" FT REGION 62..98 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 282..322 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 283..297 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 140 FT ACT_SITE 331 FT ACT_SITE 350 FT HELIX 42..46 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 50..61 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 102..106 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:3IU0" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 142..148 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 156..158 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 163..172 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 181..191 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 195..213 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 219..232 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 236..239 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:1IU4" FT HELIX 245..248 FT /evidence="ECO:0007829|PDB:3IU0" FT TURN 249..252 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 254..257 FT /evidence="ECO:0007829|PDB:3IU0" FT TURN 259..264 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 269..278 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 288..293 FT /evidence="ECO:0007829|PDB:3IU0" FT TURN 296..299 FT /evidence="ECO:0007829|PDB:1IU4" FT TURN 303..305 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 321..324 FT /evidence="ECO:0007829|PDB:1IU4" FT STRAND 331..336 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 347..353 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 359..363 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 365..370 FT /evidence="ECO:0007829|PDB:3IU0" FT HELIX 371..375 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 382..392 FT /evidence="ECO:0007829|PDB:3IU0" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:3IU0" SQ SEQUENCE 407 AA; 45684 MW; 10F7F7A04EAB2DF4 CRC64; MRIRRRALVF ATMSAVLCTA GFMPSAGEAA ADNGAGEETK SYAETYRLTA DDVANINALN ESAPAASSAG PSFRAPDSDD RVTPPAEPLD RMPDPYRPSY GRAETVVNNY IRKWQQVYSH RDGRKQQMTE EQREWLSYGC VGVTWVNSGQ YPTNRLAFAS FDEDRFKNEL KNGRPRSGET RAEFEGRVAK ESFDEEKGFQ RAREVASVMN RALENAHDES AYLDNLKKEL ANGNDALRNE DARSPFYSAL RNTPSFKERN GGNHDPSRMK AVIYSKHFWS GQDRSSSADK RKYGDPDAFR PAPGTGLVDM SRDRNIPRSP TSPGEGFVNF DYGWFGAQTE ADADKTVWTH GNHYHAPNGS LGAMHVYESK FRNWSEGYSD FDRGAYVITF IPKSWNTAPD KVKQGWP //