TGL_BACSU
ID TGL_BACSU Reviewed; 245 AA.
AC P40746;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase;
DE EC=2.3.2.13;
DE AltName: Full=Transglutaminase;
DE Short=TGase;
GN Name=tgl; Synonyms=yugV, yuxF; OrderedLocusNames=BSU31270;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9274030; DOI=10.1099/00221287-143-8-2769;
RA Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL Microbiology 143:2769-2774(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RC STRAIN=168 / OI1085;
RX PubMed=8188684; DOI=10.1016/s0021-9258(17)36752-2;
RA Hanlon D.W., Ordal G.W.;
RT "Cloning and characterization of genes encoding methyl-accepting chemotaxis
RT proteins in Bacillus subtilis.";
RL J. Biol. Chem. 269:14038-14046(1994).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9692191; DOI=10.1271/bbb.62.1109;
RA Kobayashi K., Hashiguchi K., Yokozeki K., Yamanaka S.;
RT "Molecular cloning of the transglutaminase gene from Bacillus subtilis and
RT its expression in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 62:1109-1114(1998).
RN [5]
RP CHARACTERIZATION.
RX PubMed=12501297; DOI=10.2323/jgam.44.85;
RA Kobayashi K., Suzuki S.I., Izawa Y., Miwa K., Yamanaka S.;
RT "Transglutaminase in sporulating cells of Bacillus subtilis.";
RL J. Gen. Appl. Microbiol. 44:85-91(1998).
RN [6]
RP RELATIONSHIP BETWEEN YABG AND TGL, AND DISRUPTION PHENOTYPE.
RX PubMed=16751597; DOI=10.1093/jb/mvj096;
RA Kuwana R., Okuda N., Takamatsu H., Watabe K.;
RT "Modification of GerQ reveals a functional relationship between Tgl and
RT YabG in the coat of Bacillus subtilis spores.";
RL J. Biochem. 139:887-901(2006).
CC -!- FUNCTION: Probably plays a role in the assembly of the spore coat
CC proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. In
CC wild-type spores at 37 degrees Celsius, tgl mediates the cross-linking
CC of GerQ in higher molecular mass forms, probably in cooperation with
CC YabG.
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 -!- DEVELOPMENTAL STAGE: Expressed during sporulation.
CC -!- DISRUPTION PHENOTYPE: In cells missing this gene some GerQ multimers
CC are present, indicating that tgl is not essential. Heat treatment for
CC 20 minutes at 60 degrees Celsius, which maximally activates the Tgl
CC enzymatic activity, causes cross-linking of GerQ in isolated yabG-
CC deleted spores but not in tgl/yabG double-mutant spores. Additionally,
CC the germination frequency of the tgl/yabG double-mutant spores in the
CC presence of L-alanine with or without heat activation at 60 degrees
CC Celsius is lower than that of wild-type spores.
CC {ECO:0000269|PubMed:16751597}.
CC -!- SIMILARITY: Belongs to the bacillus TGase family. {ECO:0000305}.
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DR EMBL; Z93935; CAB07928.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15105.1; -; Genomic_DNA.
DR EMBL; L29189; AAA20553.1; -; Genomic_DNA.
DR PIR; JE0179; JE0179.
DR RefSeq; NP_391005.1; NC_000964.3.
DR RefSeq; WP_003243977.1; NZ_JNCM01000033.1.
DR PDB; 4P8I; X-ray; 1.85 A; A/B=1-245.
DR PDB; 4PA5; X-ray; 1.86 A; A/B=1-245.
DR PDBsum; 4P8I; -.
DR PDBsum; 4PA5; -.
DR AlphaFoldDB; P40746; -.
DR SMR; P40746; -.
DR STRING; 224308.BSU31270; -.
DR PaxDb; P40746; -.
DR PRIDE; P40746; -.
DR EnsemblBacteria; CAB15105; CAB15105; BSU_31270.
DR GeneID; 937158; -.
DR KEGG; bsu:BSU31270; -.
DR PATRIC; fig|224308.179.peg.3387; -.
DR eggNOG; ENOG502Z8C5; Bacteria.
DR InParanoid; P40746; -.
DR OMA; FYAFECA; -.
DR BioCyc; BSUB:BSU31270-MON; -.
DR BRENDA; 2.3.2.13; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00727; Tgl; 1.
DR InterPro; IPR020916; Gln_gamma-glutamylTfrase_bac.
DR Pfam; PF20085; TGL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Sporulation;
KW Transferase.
FT CHAIN 1..245
FT /note="Protein-glutamine gamma-glutamyltransferase"
FT /id="PRO_0000213725"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 42..65
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4P8I"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 116..132
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4P8I"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:4P8I"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:4P8I"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:4P8I"
SQ SEQUENCE 245 AA; 28296 MW; 2FB36C0F83DF162C CRC64;
MIIVSGQLLR PQDIENWQID QDLNPLLKEM IETPVQFDYH SIAELMFELK LRMNIVAAAK
TLHKSGAKFA TFLKTYGNTT YWRVSPEGAL ELKYRMPPSK AIRDIAENGP FYAFECATAI
VIIYYLALID TIGEDKFNAS FDRIILYDWH YEKLPIYTET GHHFFLGDCL YFKNPEFDPQ
KAQWRGENVI LLGEDKYFAH GLGILNGKQI IDKLNSFRKK GALQSAYLLS QATRLDVPSL
FRIVR
