O05218 (YWRD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative gamma-glutamyltransferase YwrD
EC=2.3.2.2

Alternative name(s):
Glutathione hydrolase
EC=3.4.19.13

Cleaved into the following 2 chains:

1. Gamma-glutamyltranspeptidase large chain
2. Gamma-glutamyltranspeptidase small chain

Gene names

Name:	ywrD
Ordered Locus Names:	BSU36100

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid. Glutathione + H2O = L-cysteinylglycine + L-glutamate.
Subunit structure	This enzyme consists of two polypeptide chains, which are synthesized from a single polypeptide By similarity.
Induction	Positively regulated by TnrA under nitrogen-limited conditions. Ref.3
Miscellaneous	Is not involved in the utilization of extracellular glutathione as a sulfur source.
Sequence similarities	Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
Molecular function	Acyltransferase Hydrolase Transferase
PTM	Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	gamma-glutamyltransferase activity Inferred from electronic annotation. Source: EC hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	Gamma-glutamyltranspeptidase large chain		PRO_0000360767
	Chain	339 – 525	187	Gamma-glutamyltranspeptidase small chain		PRO_0000360768

Sequences

	Sequence		Length	Mass (Da)
	O05218 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 6E430B67757CC81A	FASTA	525	57,487
	10 20 30 40 50 60 MNKSVIGTKQ MVVSPHYLAS QAGNRILDKG GNAFDAAVAV SACLAVVYPH MTGLGGDSFW 70 80 90 100 110 120 LTFHQETKAV KVYNGSGRSG KNVTRDVYKG KSAIPLRGID SAITVPGMVD SWDAVLKEYG 130 140 150 160 170 180 RLSLADVLEP ARDYAQNGFP VSADQCRHTE KNIELLASTP YTADIFTRRG KAPVPGERFV 190 200 210 220 230 240 QKELADSLNL IAEKGRSAFY EGDLAQRIVS HLQNNGSYMT IDDFKAHRGE WAAPVSSDYR 250 260 270 280 290 300 GYSVYQAPPN SQGFTGLLTL NILENYDFTQ IEHGSFEYYH VLVEALKKSF LDRDAVLTDP 310 320 330 340 350 360 AFADIPLERL LDKRYAKQLA EEIGYLAIPA ESRPVGSDTA YAAVIDADGN AVSFIQSLYF 370 380 390 400 410 420 EFGSAVTAGD TGILLQNRGS FFSLDENHVN TLEPRKRTFH TLMPAMVCKG GKPKILYGTQ 430 440 450 460 470 480 GGEGQPQTQT AIITRMLDYG MHPQQAISEP RWVWGRTWGE EYEGLRVEGR FTDKTIQKLK 490 500 510 520 DSGHLVEVVG DYDPLMGQAA AIKVDEEGFL QGGADPRGDG AAVGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)." Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P. Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box." Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y. Mol. Microbiol. 49:157-165(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY TNRA.
[4]	"Gamma-glutamyltranspeptidase, but not YwrD, is important in utilization of extracellular glutathione as a sulfur source in Bacillus subtilis." Minami H., Suzuki H., Kumagai H. J. Bacteriol. 186:1213-1214(2004) [PubMed] [Europe PMC] [Abstract] Cited for: LACK OF FUNCTION IN GLUTATHIONE METABOLISM.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z93767 Genomic DNA. Translation: CAB07790.1. AL009126 Genomic DNA. Translation: CAB15627.1.
PIR	F70068.
RefSeq	NP_391491.1. NC_000964.3.
3D structure databases
HSSP	HSSP built from PDB template 2DG5 based on UniProtKB P18956.
ProteinModelPortal	O05218.
SMR	O05218. Positions 2-525.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU36100.
Protein family/group databases
MEROPS	T03.A09.
Proteomic databases
PaxDb	O05218.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB15627; CAB15627; BSU36100.
GeneID	936884.
KEGG	bsu:BSU36100.
PATRIC	18979238. VBIBacSub10457_3781.
Organism-specific databases
GenoList	BSU36100.
Phylogenomic databases
eggNOG	COG0405.
HOGENOM	HOG000175618.
KO	K00681.
OMA	NAVSFIQ.
ProtClustDB	CLSK888003.
Enzyme and pathway databases
BioCyc	BSUB:BSU36100-MONOMER.
Family and domain databases
InterPro	IPR000101. GGT_peptidase. [Graphical view]
PANTHER	PTHR11686. PTHR11686. 1 hit.
Pfam	PF01019. G_glu_transpept. 1 hit. [Graphical view]
PRINTS	PR01210. GGTRANSPTASE.
TIGRFAMs	TIGR00066. g_glut_trans. 1 hit.
PROSITE	PS00462. G_GLU_TRANSPEPTIDASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YWRD_BACSU

Accession

Primary (citable) accession number: O05218
Secondary accession number(s): Q795C4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program