TGAS_STRMB
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 25-MAY-2022, entry version 92.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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 / VKM
RC 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}.
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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 PRIDE; P81453; -.
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; -; 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; SSF54001; 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
