ID GGT_ECOLI STANDARD; PRT; 580 AA. AC P18956; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Gamma-glutamyltranspeptidase precursor (EC 2.3.2.2). GN GGT OR B3447. OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 26-41 AND 391-403. RC STRAIN=K12; RX MEDLINE=89359163; PubMed=2570061; RA Suzuki H., Kumagai H., Echigo T., Tochikura T.; RT "DNA sequence of the Escherichia coli K-12 RT gamma-glutamyltranspeptidase gene, ggt."; RL J. Bacteriol. 171:5169-5172(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] RP SEQUENCE OF 1-362 FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=94316500; PubMed=8041620; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the RT region from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [4] RP MUTAGENESIS. RX MEDLINE=93080553; PubMed=1360205; RA Hashimoto W., Suzuki H., Nohara S., Kumagai H.; RT "Escherichia coli gamma-glutamyltranspeptidase mutants deficient in RT processing to subunits."; RL Biochem. Biophys. Res. Commun. 189:173-178(1992). CC -!- CATALYTIC ACTIVITY: (5-L-glutamyl)-peptide + an amino acid = CC peptide + 5-L-glutamyl-amino acid. CC -!- PATHWAY: GGT plays a key role in the gamma-glutamyl cycle, a CC pathway for the synthesis and degradation of glutathione. CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are CC synthesized in precursor form from a single polypeptide. CC -!- SUBCELLULAR LOCATION: Periplasmic. CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M28722; AAA23869.1; -. DR EMBL; U18997; AAA58245.1; -. DR EMBL; AE000421; AAC76472.1; -. DR EMBL; U00039; AAB18422.1; -. DR PIR; JV0028; EKECEX. DR MEROPS; T03.001; -. DR EcoGene; EG10374; ggt. DR InterPro; IPR000101; Peptidase_T3. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF01019; G_glu_transpept; 1. DR PRINTS; PR01210; GGTRANSPTASE. DR TIGRFAMs; TIGR00066; g_glut_trans; 1. DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1. KW Transferase; Acyltransferase; Periplasmic; Zymogen; Signal; KW Glutathione biosynthesis; Complete proteome; KW Direct protein sequencing. FT SIGNAL 1 25 FT CHAIN 26 390 Gamma-glutamyltransferase large chain. FT CHAIN 391 580 Gamma-glutamyltransferase small chain. FT BINDING 465 465 Gamma-glutamyl (Potential). FT MUTAGEN 513 513 R->A: Not processed into its subunits. FT MUTAGEN 571 571 R->G: Not processed into its subunits. SQ SEQUENCE 580 AA; 61768 MW; 772F652EBA2A5F00 CRC64; MIKPTFLRRV AIAALLSGSC FSAAAAPPAP PVSYGVEEDV FHPVRAKQGM VASVDATATQ VGVDILKEGG NAVDAAVAVG YALAVTHPQA GNLGGGGFML IRSKNGNTTA IDFREMAPAK ATRDMFLDDQ GNPDSKKSLT SHLASGTPGT VAGFSLALDK YGTMPLNKVV QPAFKLARDG FIVNDALADD LKTYGSEVLP NHENSKAIFW KEGEPLKKGD TLVQANLAKS LEMIAENGPD EFYKGTIAEQ IAQEMQKNGG LITKEDLAAY KAVERTPISG DYRGYQVYSM PPPSSGGIHI VQILNILENF DMKKYGFGSA DAMQIMAEAE KYAYADRSEY LGDPDFVKVP WQALTNKAYA KSIADQIDIN KAKPSSEIRP GKLAPYESNQ TTHYSVVDKD GNAVAVTYTL NTTFGTGIVA GESGILLNNQ MDDFSAKPGV PNVYGLVGGD ANAVGPNKRP LSSMSPTIVV KDGKTWLVTG SPGGSRIITT VLQMVVNSID YGLNVAEATN APRFHHQWLP DELRVEKGFS PDTLKLLEAK GQKVALKEAM GSTQSIMVGP DGELYGASDP RSVDDLTAGY //