YWRD_BACSU
ID YWRD_BACSU Reviewed; 525 AA.
AC O05218; Q795C4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Glutathione hydrolase-like YwrD proenzyme;
DE EC=2.3.2.2;
DE AltName: Full=Putative gamma-glutamyltransferase YwrD;
DE EC=3.4.19.13;
DE Contains:
DE RecName: Full=Glutathione hydrolase-like YwrD large chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase-like YwrD small chain;
GN Name=ywrD; OrderedLocusNames=BSU36100;
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=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(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 INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
RN [4]
RP LACK OF FUNCTION IN GLUTATHIONE METABOLISM, AND 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).
CC -!- FUNCTION: Overexpressed protein with an N-terminal His tag has been
CC reported not to hydrolyze glutathione; it is not clear if the construct
CC is processed to 2 subunits (PubMed:14762019).
CC {ECO:0000305|PubMed:14762019}.
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 -!- 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 -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
CC synthesized from a single polypeptide. {ECO:0000250}.
CC -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC conditions. {ECO:0000269|PubMed:12823818}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Grows normally with glutathione as a sulfur
CC source. {ECO:0000269|PubMed:14762019}.
CC -!- MISCELLANEOUS: Is not involved in the utilization of extracellular
CC glutathione as a sulfur source. {ECO:0000269|PubMed:14762019}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Z93767; CAB07790.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15627.1; -; Genomic_DNA.
DR PIR; F70068; F70068.
DR RefSeq; NP_391491.1; NC_000964.3.
DR RefSeq; WP_003227847.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; O05218; -.
DR SMR; O05218; -.
DR STRING; 224308.BSU36100; -.
DR MEROPS; T03.025; -.
DR PaxDb; O05218; -.
DR PRIDE; O05218; -.
DR DNASU; 936884; -.
DR EnsemblBacteria; CAB15627; CAB15627; BSU_36100.
DR GeneID; 936884; -.
DR KEGG; bsu:BSU36100; -.
DR PATRIC; fig|224308.179.peg.3907; -.
DR eggNOG; COG0405; Bacteria.
DR InParanoid; O05218; -.
DR OMA; FMVIGSP; -.
DR PhylomeDB; O05218; -.
DR BioCyc; BSUB:BSU36100-MON; -.
DR Proteomes; UP000001570; Chromosome.
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: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.
PE 1: Evidence at protein level;
KW Acyltransferase; Hydrolase; Protease; Reference proteome; Transferase;
KW Zymogen.
FT CHAIN 1..338
FT /note="Glutathione hydrolase-like YwrD large chain"
FT /id="PRO_0000360767"
FT CHAIN 339..525
FT /note="Glutathione hydrolase-like YwrD small chain"
FT /id="PRO_0000360768"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 525 AA; 57487 MW; 6E430B67757CC81A CRC64;
MNKSVIGTKQ MVVSPHYLAS QAGNRILDKG GNAFDAAVAV SACLAVVYPH MTGLGGDSFW
LTFHQETKAV KVYNGSGRSG KNVTRDVYKG KSAIPLRGID SAITVPGMVD SWDAVLKEYG
RLSLADVLEP ARDYAQNGFP VSADQCRHTE KNIELLASTP YTADIFTRRG KAPVPGERFV
QKELADSLNL IAEKGRSAFY EGDLAQRIVS HLQNNGSYMT IDDFKAHRGE WAAPVSSDYR
GYSVYQAPPN SQGFTGLLTL NILENYDFTQ IEHGSFEYYH VLVEALKKSF LDRDAVLTDP
AFADIPLERL LDKRYAKQLA EEIGYLAIPA ESRPVGSDTA YAAVIDADGN AVSFIQSLYF
EFGSAVTAGD TGILLQNRGS FFSLDENHVN TLEPRKRTFH TLMPAMVCKG GKPKILYGTQ
GGEGQPQTQT AIITRMLDYG MHPQQAISEP RWVWGRTWGE EYEGLRVEGR FTDKTIQKLK
DSGHLVEVVG DYDPLMGQAA AIKVDEEGFL QGGADPRGDG AAVGI
