ID GGT_ECOLI Reviewed; 580 AA. AC P18956; Q2M7B0; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 11-JUN-2014, entry version 131. DE RecName: Full=Gamma-glutamyltranspeptidase; DE EC=2.3.2.2; DE AltName: Full=Glutathione hydrolase; DE EC=3.4.19.13; DE Contains: DE RecName: Full=Gamma-glutamyltranspeptidase large chain; DE Contains: DE RecName: Full=Gamma-glutamyltranspeptidase small chain; DE Flags: Precursor; GN Name=ggt; OrderedLocusNames=b3447, JW3412; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-41 AND RP 391-403. RC STRAIN=K12; RX PubMed=2570061; RA Suzuki H., Kumagai H., Echigo T., Tochikura T.; RT "DNA sequence of the Escherichia coli K-12 gamma- RT glutamyltranspeptidase gene, ggt."; RL J. Bacteriol. 171:5169-5172(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; 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 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-362. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8041620; DOI=10.1093/nar/22.13.2576; 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 [5] RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF RP ARG-513 AND ARG-571, AND AUTOCATALYTIC CLEAVAGE. RX PubMed=1360205; DOI=10.1016/0006-291X(92)91540-7; 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). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-580 IN COMPLEX WITH RP GLUTAMATE, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AND AUTOCATALYTIC RP CLEAVAGE. RX PubMed=16618936; DOI=10.1073/pnas.0511020103; RA Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.; RT "Crystal structures of gamma-glutamyltranspeptidase from Escherichia RT coli, a key enzyme in glutathione metabolism, and its reaction RT intermediate."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6471-6476(2006). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-580 OF MUTANT ALA-391, RP SUBUNIT, AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF THR-391. RX PubMed=17135273; DOI=10.1074/jbc.M607490200; RA Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.; RT "Crystal structure of the gamma-glutamyltranspeptidase precursor RT protein from Escherichia coli. Structural changes upon autocatalytic RT processing and implications for the maturation mechanism."; RL J. Biol. Chem. 282:2433-2439(2007). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 25-580 IN COMPLEXES WITH RP AZASERINE AND ACIVICIN, ACTIVE SITE, SUBUNIT, AND AUTOCATALYTIC RP CLEAVAGE. RX PubMed=18555071; DOI=10.1016/j.jmb.2008.05.007; RA Wada K., Hiratake J., Irie M., Okada T., Yamada C., Kumagai H., RA Suzuki H., Fukuyama K.; RT "Crystal structures of Escherichia coli gamma-glutamyltranspeptidase RT in complex with azaserine and acivicin: novel mechanistic implication RT for inhibition by glutamine antagonists."; RL J. Mol. Biol. 380:361-372(2008). CC -!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a CC peptide + a 5-L-glutamyl amino acid. CC -!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L- CC glutamate. 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 -!- SUBCELLULAR LOCATION: Periplasm. CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit. 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; -; Genomic_DNA. DR EMBL; U18997; AAA58245.1; -; Genomic_DNA. DR EMBL; U00096; AAC76472.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77846.1; -; Genomic_DNA. DR EMBL; U00039; AAB18422.1; -; Genomic_DNA. DR PIR; JV0028; EKECEX. DR RefSeq; NP_417904.1; NC_000913.3. DR RefSeq; YP_491987.1; NC_007779.1. DR PDB; 2DBU; X-ray; 1.95 A; A/C=25-390, B/D=391-580. DR PDB; 2DBW; X-ray; 1.80 A; A/C=25-390, B/D=391-580. DR PDB; 2DBX; X-ray; 1.70 A; A/C=25-390, B/D=391-580. DR PDB; 2DG5; X-ray; 1.60 A; A/C=25-390, B/D=391-580. DR PDB; 2E0W; X-ray; 2.55 A; A/B=25-580. DR PDB; 2E0X; X-ray; 1.95 A; A/C=25-390, B/D=391-580. DR PDB; 2E0Y; X-ray; 2.02 A; A/C=25-390, B/D=391-580. DR PDB; 2Z8I; X-ray; 1.65 A; A/C=25-390, B/D=391-580. DR PDB; 2Z8J; X-ray; 2.05 A; A/C=25-390, B/D=391-580. DR PDB; 2Z8K; X-ray; 1.65 A; A/C=25-390, B/D=391-580. DR PDBsum; 2DBU; -. DR PDBsum; 2DBW; -. DR PDBsum; 2DBX; -. DR PDBsum; 2DG5; -. DR PDBsum; 2E0W; -. DR PDBsum; 2E0X; -. DR PDBsum; 2E0Y; -. DR PDBsum; 2Z8I; -. DR PDBsum; 2Z8J; -. DR PDBsum; 2Z8K; -. DR ProteinModelPortal; P18956; -. DR DIP; DIP-9758N; -. DR IntAct; P18956; 1. DR MINT; MINT-1260227; -. DR STRING; 511145.b3447; -. DR DrugBank; DB01212; Ceftriaxone. DR MEROPS; T03.001; -. DR PaxDb; P18956; -. DR EnsemblBacteria; AAC76472; AAC76472; b3447. DR EnsemblBacteria; BAE77846; BAE77846; BAE77846. DR GeneID; 12932672; -. DR GeneID; 947947; -. DR KEGG; ecj:Y75_p3731; -. DR KEGG; eco:b3447; -. DR PATRIC; 32122334; VBIEscCol129921_3544. DR EchoBASE; EB0369; -. DR EcoGene; EG10374; ggt. DR eggNOG; COG0405; -. DR HOGENOM; HOG000175617; -. DR KO; K00681; -. DR OMA; AHPLATH; -. DR OrthoDB; EOG62K1RV; -. DR PhylomeDB; P18956; -. DR BioCyc; EcoCyc:EG10374-MONOMER; -. DR BioCyc; ECOL316407:JW3412-MONOMER; -. DR BioCyc; MetaCyc:EG10374-MONOMER; -. DR SABIO-RK; P18956; -. DR UniPathway; UPA00204; -. DR EvolutionaryTrace; P18956; -. DR PRO; PR:P18956; -. DR Genevestigator; P18956; -. DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki. DR GO; GO:0003840; F:gamma-glutamyltransferase activity; IDA:EcoliWiki. DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR000101; GGT_peptidase. DR InterPro; IPR029055; Ntn_hydrolases_N. DR PANTHER; PTHR11686; PTHR11686; 1. DR Pfam; PF01019; G_glu_transpept; 1. DR PRINTS; PR01210; GGTRANSPTASE. 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; Complete proteome; KW Direct protein sequencing; Glutathione biosynthesis; Hydrolase; KW Periplasm; Protease; Reference proteome; Signal; Transferase; Zymogen. FT SIGNAL 1 25 FT CHAIN 26 390 Gamma-glutamyltranspeptidase large chain. FT /FTId=PRO_0000011052. FT CHAIN 391 580 Gamma-glutamyltranspeptidase small chain. FT /FTId=PRO_0000011053. FT REGION 462 463 Glutamate binding. FT REGION 483 484 Glutamate binding. FT ACT_SITE 391 391 Nucleophile. FT BINDING 114 114 Glutamate. FT BINDING 409 409 Glutamate. FT BINDING 411 411 Glutamate. FT BINDING 430 430 Glutamate. FT BINDING 433 433 Glutamate. FT MUTAGEN 391 391 T->A: Abolishes autocatalytic cleavage. FT MUTAGEN 513 513 R->A: Not processed into its subunits. FT MUTAGEN 571 571 R->G: Not processed into its subunits. FT STRAND 39 41 FT STRAND 44 48 FT STRAND 50 54 FT HELIX 56 67 FT HELIX 72 86 FT TURN 88 90 FT STRAND 93 102 FT STRAND 108 113 FT TURN 123 126 FT STRAND 129 131 FT HELIX 135 139 FT HELIX 142 144 FT HELIX 150 161 FT HELIX 166 179 FT HELIX 185 193 FT HELIX 195 197 FT HELIX 199 201 FT HELIX 203 209 FT HELIX 225 237 FT HELIX 240 243 FT HELIX 246 257 FT HELIX 264 269 FT STRAND 273 275 FT STRAND 278 282 FT STRAND 285 289 FT HELIX 296 307 FT HELIX 312 315 FT HELIX 320 340 FT TURN 344 346 FT HELIX 351 354 FT HELIX 357 364 FT HELIX 375 377 FT HELIX 384 386 FT STRAND 392 397 FT STRAND 403 409 FT TURN 413 416 FT HELIX 421 423 FT HELIX 430 433 FT STRAND 434 437 FT STRAND 467 471 FT STRAND 474 479 FT HELIX 484 486 FT HELIX 487 499 FT HELIX 505 510 FT STRAND 518 520 FT STRAND 523 525 FT HELIX 531 539 FT STRAND 544 546 FT STRAND 554 558 FT STRAND 564 568 FT STRAND 576 579 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 //