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UniProtKB/Swiss-Prot entry P40746


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TGL_BACSU
Primary accession number P40746
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on July 15, 1998 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 48)
Name and origin of the protein
Protein name Protein-glutamine gamma-glutamyltransferase
Synonyms EC 2.3.2.13
Transglutaminase
TGase
Gene name
Name: tgl
Synonyms: yugV, yuxF
OrderedLocusNames: BSU31270
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9274030 [NCBI, ExPASy, EBI, Israel, Japan]
Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H., Duesterhoeft A., Pohl T.M., Weitzenegger T.;
"Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
Microbiology 143:2769-2774(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
STRAIN=168 / OI1085;
PubMed=8188684 [NCBI, ExPASy, EBI, Israel, Japan]
Hanlon D.W., Ordal G.W.;
"Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis.";
J. Biol. Chem. 269:14038-14046(1994).
[4]
CHARACTERIZATION.
PubMed=9692191 [NCBI, ExPASy, EBI, Israel, Japan]
Kobayashi K., Hashiguchi K., Yokozeki K., Yamanaka S.;
"Molecular cloning of the transglutaminase gene from Bacillus subtilis and its expression in Escherichia coli.";
Biosci. Biotechnol. Biochem. 62:1109-1114(1998).
[5]
CHARACTERIZATION.
PubMed=12501297 [NCBI, ExPASy, EBI, Israel, Japan]
Kobayashi K., Suzuki S.I., Izawa Y., Miwa K., Yamanaka S.;
"Transglutaminase in sporulating cells of Bacillus subtilis.";
J. Gen. Appl. Microbiol. 44:85-91(1998).
[6]
RELATIONSHIP BETWEEN YABG AND TGL.
DOI=10.1093/jb/mvj096; PubMed=16751597 [NCBI, ExPASy, EBI, Israel, Japan]
Kuwana R., Okuda N., Takamatsu H., Watabe K.;
"Modification of GerQ reveals a functional relationship between Tgl and YabG in the coat of Bacillus subtilis spores.";
J. Biochem. 139:887-901(2006).
Comments
  • FUNCTION: Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. Mediates the cross-linking of gerQ, probably in cooperation with yabG.
  • CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N5-alkylglutamine + NH3.
  • DEVELOPMENTAL STAGE: Expressed during sporulation.
  • MISCELLANEOUS: In wild-type spores at 37 degrees Celsius, tgl mediates the cross-linking of gerQ in higher molecular mass forms. Some gerQ multimers are found in tgl mutant spores, indicating that tgl is not essential. Heat treatment for 20 minutes at 60 degrees Celsius, which maximally activates the tgl enzymatic activity, causes cross-linking of gerQ in isolated yabG spores but not in tgl/yabG double-mutant spores. Additionally, the germination frequency of the tgl/yabG double-mutant spores in the presence of L-alanine with or without heat activation at 60 degrees Celsius is lower that of wild-type spores.
  • SIMILARITY: Belongs to the bacillus 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
Z93935; CAB07928.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99119; CAB15105.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L29189; AAA20553.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JE0179; JE0179.
RefSeq NP_391005.1; -.
3D structure databases
ModBase P40746.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3122-MON; -.
Organism-specific databases
SubtiList BG10946; tgl. [Micado]
Ontologies
GO
GO:0003810; Molecular function: protein-glutamine gamma-glutamyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0030435; Biological process: sporulation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00727; -; 1.
PBIL [Tree]
BLOCKS P40746.
Genome annotation databases
GeneID 937158; -.
GenomeReviews AL009126_GR; BSU31270.
KEGG bsu:BSU31270; -.
NMPDR fig|224308.1.peg.3130; -.
Phylogenomic databases
HOGENOM P40746; -.
Genome annotation databases
CMR P40746; BSU31270.
Other
ProtoNet P40746.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Complete proteome; Sporulation; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   245  245     Protein-glutamine gamma-glutamyltransferase. PRO_0000213725
Sequence information
Length: 245 AA [This is the length of the unprocessed precursor] Molecular weight: 28296 Da [This is the MW of the unprocessed precursor] CRC64: 2FB36C0F83DF162C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIIVSGQLLR PQDIENWQID QDLNPLLKEM IETPVQFDYH SIAELMFELK LRMNIVAAAK 

        70         80         90        100        110        120 
TLHKSGAKFA TFLKTYGNTT YWRVSPEGAL ELKYRMPPSK AIRDIAENGP FYAFECATAI 

       130        140        150        160        170        180 
VIIYYLALID TIGEDKFNAS FDRIILYDWH YEKLPIYTET GHHFFLGDCL YFKNPEFDPQ 

       190        200        210        220        230        240 
KAQWRGENVI LLGEDKYFAH GLGILNGKQI IDKLNSFRKK GALQSAYLLS QATRLDVPSL 


FRIVR 

P40746 in FASTA format

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