GGT_BACSU
ID GGT_BACSU Reviewed; 587 AA.
AC P54422;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutathione hydrolase proenzyme;
DE EC=3.4.19.13;
DE AltName: Full=Gamma-glutamyltranspeptidase proenzyme;
DE EC=2.3.2.2 {ECO:0000269|PubMed:20088880};
DE Contains:
DE RecName: Full=Glutathione hydrolase large chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase small chain;
DE Flags: Precursor;
GN Name=ggt; OrderedLocusNames=BSU18410;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=168 / JH642;
RX PubMed=8763966; DOI=10.1128/jb.178.14.4319-4322.1996;
RA Xu K., Strauch M.A.;
RT "Identification, sequence, and expression of the gene encoding gamma-
RT glutamyltranspeptidase in Bacillus subtilis.";
RL J. Bacteriol. 178:4319-4322(1996).
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 DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=14762019; DOI=10.1128/jb.186.4.1213-1214.2004;
RA Minami H., Suzuki H., Kumagai H.;
RT "Gamma-glutamyltranspeptidase, but not YwrD, is important in utilization of
RT extracellular glutathione as a sulfur source in Bacillus subtilis.";
RL J. Bacteriol. 186:1213-1214(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 36-587 IN COMPLEX WITH GLUTAMATE,
RP CATALYTIC ACTIVITY, SUBUNIT, AND AUTOCATALYTIC CLEAVAGE.
RX PubMed=20088880; DOI=10.1111/j.1742-4658.2009.07543.x;
RA Wada K., Irie M., Suzuki H., Fukuyama K.;
RT "Crystal structure of the halotolerant gamma-glutamyltranspeptidase from
RT Bacillus subtilis in complex with glutamate reveals a unique architecture
RT of the solvent-exposed catalytic pocket.";
RL FEBS J. 277:1000-1009(2010).
CC -!- FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione
CC (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl
CC compounds. The metabolism of glutathione releases free glutamate and
CC the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and
CC glycine by dipeptidases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC ChEBI:CHEBI:78608; EC=2.3.2.2;
CC Evidence={ECO:0000269|PubMed:20088880};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:143103; EC=3.4.19.13;
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
CC synthesized in precursor form from a single polypeptide.
CC {ECO:0000269|PubMed:20088880}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8763966}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the end of vegetative growth.
CC {ECO:0000269|PubMed:8763966}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000269|PubMed:20088880}.
CC -!- DISRUPTION PHENOTYPE: Loss of ability to grow with glutathione as a
CC sulfur source. {ECO:0000269|PubMed:14762019}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U49358; AAC44233.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13724.1; -; Genomic_DNA.
DR PIR; F69631; F69631.
DR RefSeq; NP_389723.1; NC_000964.3.
DR RefSeq; WP_003231470.1; NZ_JNCM01000036.1.
DR PDB; 2V36; X-ray; 1.85 A; A/C=29-402, B/D=403-587.
DR PDB; 3A75; X-ray; 1.95 A; A/C=36-402, B/D=403-587.
DR PDB; 3WHQ; X-ray; 1.85 A; A=1-402, B=403-587.
DR PDB; 3WHR; X-ray; 1.58 A; A=1-402, B=403-587.
DR PDB; 3WHS; X-ray; 1.80 A; A=1-402, B=403-587.
DR PDBsum; 2V36; -.
DR PDBsum; 3A75; -.
DR PDBsum; 3WHQ; -.
DR PDBsum; 3WHR; -.
DR PDBsum; 3WHS; -.
DR AlphaFoldDB; P54422; -.
DR SMR; P54422; -.
DR MINT; P54422; -.
DR STRING; 224308.BSU18410; -.
DR MEROPS; T03.001; -.
DR PaxDb; P54422; -.
DR PRIDE; P54422; -.
DR EnsemblBacteria; CAB13724; CAB13724; BSU_18410.
DR GeneID; 940001; -.
DR KEGG; bsu:BSU18410; -.
DR PATRIC; fig|224308.179.peg.2008; -.
DR eggNOG; COG0405; Bacteria.
DR InParanoid; P54422; -.
DR OMA; KATKNMF; -.
DR PhylomeDB; P54422; -.
DR BioCyc; BSUB:BSU18410-MON; -.
DR BRENDA; 2.3.2.2; 658.
DR BRENDA; 3.4.19.13; 658.
DR UniPathway; UPA00204; -.
DR EvolutionaryTrace; P54422; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Glutathione biosynthesis; Hydrolase;
KW Protease; Reference proteome; Secreted; Signal; Transferase; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..35
FT /evidence="ECO:0000255"
FT /id="PRO_0000011049"
FT CHAIN 36..402
FT /note="Glutathione hydrolase large chain"
FT /id="PRO_0000011050"
FT CHAIN 403..587
FT /note="Glutathione hydrolase small chain"
FT /id="PRO_0000011051"
FT ACT_SITE 403
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:20088880"
FT BINDING 113
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20088880"
FT BINDING 421
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20088880"
FT BINDING 442
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20088880"
FT BINDING 445
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20088880"
FT BINDING 464..465
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20088880,
FT ECO:0007744|PDB:3A75"
FT BINDING 485..486
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20088880,
FT ECO:0007744|PDB:3A75"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2V36"
FT STRAND 39..53
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:3WHR"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3WHR"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3WHR"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2V36"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 318..338
FT /evidence="ECO:0007829|PDB:3WHR"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:3WHR"
FT TURN 425..428
FT /evidence="ECO:0007829|PDB:3WHR"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 488..501
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 507..512
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:3WHR"
FT HELIX 532..540
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:3WHR"
FT TURN 562..565
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:3WHR"
FT TURN 573..576
FT /evidence="ECO:0007829|PDB:3WHR"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:3WHR"
SQ SEQUENCE 587 AA; 64189 MW; 6BF200CBA882C4F6 CRC64;
MKRTWNVCLT ALLSVLLVAG SVPFHAEAKK PPKSYDEYKQ VDVGKDGMVA TAHPLASEIG
ADVLKKGGNA IDAAVAIQFA LNVTEPMMSG IGGGGFMMVY DGKTKDTTII DSRERAPAGA
TPDMFLDENG KAIPFSERVT KGTAVGVPGT LKGLEEALDK WGTRSMKQLI TPSIKLAEKG
FPIDSVLAEA ISDYQEKLSR TAAKDVFLPN GEPLKEGDTL IQKDLAKTFK LIRSKGTDAF
YKGKFAKTLS DTVQDFGGSM TEKDLENYDI TIDEPIWGDY QGYQIATTPP PSSGGIFLLQ
MLKILDHFNL SQYDVRSWEK YQLLAETMHL SYADRASYAG DPEFVNVPLK GLLHPDYIKE
RQQLINLDQV NKKPKAGDPW KYQEGSANYK QVEQPKDKVE GQTTHFTVAD RWGNVVSYTT
TIEQLFGTGI MVPDYGVILN NELTDFDAIP GGANEVQPNK RPLSSMTPTI LFKDDKPVLT
VGSPGGATII SSVLQTILYH IEYGMELKAA VEEPRIYTNS MSSYRYEDGV PKDVLSKLNG
MGHKFGTSPV DIGNVQSISI DHENGTFKGV ADSSRNGAAI GINLKRK
