[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / IFO 13819 / NCIMB 11159; DOI=10.1128/AEM.69.1.358-366.2003; PubMed=12514016 [NCBI, ExPASy, EBI, Israel, Japan] Kikuchi Y., Date M., Yokoyama K., Umezawa Y., Matsui H.; "Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus."; Appl. Environ. Microbiol. 69:358-366(2003).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-407, AND PARTIAL PROTEIN SEQUENCE. STRAIN=ATCC 27441 / CBS 777.72 / DSM 40587 / IFO 13476 / JCM 4778; PubMed=9839945 [NCBI, ExPASy, EBI, Israel, Japan] Pasternack R., Dorsch S., Otterbach J.T., Robenek I.R., Wolf S., Fuchsbauer H.-L.; "Bacterial pro-transglutaminase from Streptoverticillium mobaraense: purification, characterisation and sequence of the zymogen."; Eur. J. Biochem. 257:570-576(1998).
[3]	PROTEIN SEQUENCE OF 77-407, AND MASS SPECTROMETRY. STRAIN=S-8112; PubMed=8099353 [NCBI, ExPASy, EBI, Israel, Japan] Kanaji T., Ozaki H., Takao T., Kawajiri H., Ide H., Motoki M., Shimonishi Y.; "Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112."; J. Biol. Chem. 268:11565-11572(1993).
[4]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-407. STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / IFO 13819 / NCIMB 11159; DOI=10.1074/jbc.M203933200; PubMed=12221081 [NCBI, ExPASy, EBI, Israel, Japan] Kashiwagi T., Yokoyama K., Ishikawa K., Ono K., Ejima D., Matsui H., Suzuki E.; "Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense."; J. Biol. Chem. 277:44252-44260(2002).

Comments

FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N⁵-alkylglutamine + NH₃.
MASS SPECTROMETRY: Mass=37869.2; Mass_error=8.8; Method=Electrospray; Range=77-407; Source=PubMed:8099353;.
BIOTECHNOLOGY: Sold under the name Activa TG by Ajinomoto. It has the ability to cross-link protein molecules present in food without the use of salt or binders. Used to improve some of the physical properties such as firmness, elasticity and moisture retention of food such as meat, poultry and seafood.
SIMILARITY: Belongs to the bacterial TGase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF531437; AAM95951.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y18315; CAA77128.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1IU4; X-ray; 2.40 A; A/B/C/D=77-407.

[ExPASy / RCSB / EBI]

PDBsum

1IU4; -.

ModBase

P81453.

Family and domain databases

InterPro

IPR015107; Transglut_prok.
Graphical view of domain structure.

Pfam

PF09017; Transglut_prok; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037210; Transglut_prok; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acyltransferase; Direct protein sequencing; Signal; Transferase; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 31`	`31`	`Potential.`
`PROPEP`	`32 76`	`45`		`PRO_0000033656`
`CHAIN`	`77 407`	`331`	`Protein-glutamine gamma-glutamyltransferase.`	`PRO_0000033657`
`ACT_SITE`	`140 140`
`ACT_SITE`	`331 331`
`ACT_SITE`	`350 350`
`STRAND`	`102 106`	`5`
`HELIX`	`107 117`	`11`
`HELIX`	`130 136`	`7`
`HELIX`	`142 148`	`7`
`STRAND`	`156 158`	`3`
`HELIX`	`163 172`	`10`
`HELIX`	`181 192`	`12`
`HELIX`	`195 211`	`17`
`TURN`	`212 215`	`4`
`HELIX`	`219 232`	`14`
`HELIX`	`236 239`	`4`
`STRAND`	`242 244`	`3`
`TURN`	`245 248`	`4`
`HELIX`	`249 252`	`4`
`TURN`	`254 257`	`4`
`STRAND`	`259 261`	`3`
`HELIX`	`266 268`	`3`
`STRAND`	`269 278`	`10`
`HELIX`	`288 293`	`6`
`TURN`	`296 299`	`4`
`TURN`	`303 305`	`3`
`STRAND`	`321 324`	`4`
`STRAND`	`329 336`	`8`
`HELIX`	`343 345`	`3`
`STRAND`	`347 353`	`7`
`STRAND`	`359 363`	`5`
`STRAND`	`365 370`	`6`
`HELIX`	`371 374`	`4`
`STRAND`	`383 392`	`10`

Sequence information

Length: 407 AA [This is the length of the unprocessed precursor]

Molecular weight: 45684 Da [This is the MW of the unprocessed precursor]

CRC64: 10F7F7A04EAB2DF4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRIRRRALVF ATMSAVLCTA GFMPSAGEAA ADNGAGEETK SYAETYRLTA DDVANINALN 

        70         80         90        100        110        120 
ESAPAASSAG PSFRAPDSDD RVTPPAEPLD RMPDPYRPSY GRAETVVNNY IRKWQQVYSH 

       130        140        150        160        170        180 
RDGRKQQMTE EQREWLSYGC VGVTWVNSGQ YPTNRLAFAS FDEDRFKNEL KNGRPRSGET 

       190        200        210        220        230        240 
RAEFEGRVAK ESFDEEKGFQ RAREVASVMN RALENAHDES AYLDNLKKEL ANGNDALRNE 

       250        260        270        280        290        300 
DARSPFYSAL RNTPSFKERN GGNHDPSRMK AVIYSKHFWS GQDRSSSADK RKYGDPDAFR 

       310        320        330        340        350        360 
PAPGTGLVDM SRDRNIPRSP TSPGEGFVNF DYGWFGAQTE ADADKTVWTH GNHYHAPNGS 

       370        380        390        400 
LGAMHVYESK FRNWSEGYSD FDRGAYVITF IPKSWNTAPD KVKQGWP

P81453 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools