Reviewed, UniProtKB/Swiss-Prot P18956 (GGT_ECOLI)

Names and origin

Protein names

Recommended name:
    Gamma-glutamyltranspeptidase
    EC=2.3.2.2
Cleaved into the following 2 chains:
    1- Recommended name:
            Gamma-glutamyltranspeptidase large chain
    2- Recommended name:
            Gamma-glutamyltranspeptidase small chain

Gene names

Name:	ggt
Ordered Locus Names:	b3447, JW3412

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	580 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	(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid.
Pathway	Sulfur metabolism; glutathione metabolism.
Subunit structure	This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Cellular component	Periplasm
Domain	Signal
Molecular function	Acyltransferase Transferase
PTM	Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glutathione biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW gamma-glutamyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.1

Chain

26 – 390

365

Gamma-glutamyltranspeptidase large chain

PRO_0000011052

Chain

391 – 580

190

Gamma-glutamyltranspeptidase small chain

PRO_0000011053

Experimental info

Mutagenesis

513

1

R → A: Not processed into its subunits.

Mutagenesis

571

1

R → G: Not processed into its subunits.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

580

Helix Strand Turn

Details...

Beta strand

39 – 41

3

Beta strand

44 – 48

5

Beta strand

50 – 54

5

Helix

56 – 67

12

Helix

72 – 86

15

Turn

88 – 90

3

Beta strand

93 – 102

10

Beta strand

108 – 113

6

Turn

123 – 126

4

Helix

135 – 139

5

Helix

142 – 144

3

Helix

150 – 161

12

Helix

166 – 179

14

Helix

185 – 193

9

Helix

195 – 197

3

Helix

199 – 201

3

Helix

203 – 209

7

Helix

225 – 237

13

Helix

240 – 243

4

Helix

246 – 256

11

Turn

257 – 259

3

Helix

264 – 269

6

Beta strand

273 – 275

3

Beta strand

278 – 282

5

Beta strand

285 – 289

5

Helix

296 – 307

12

Helix

312 – 315

4

Helix

320 – 340

21

Turn

344 – 346

3

Helix

351 – 354

4

Helix

357 – 365

9

Helix

375 – 377

3

Helix

384 – 386

3

Beta strand

392 – 397

6

Beta strand

403 – 409

7

Turn

413 – 416

4

Helix

421 – 423

3

Helix

430 – 433

4

Beta strand

434 – 437

4

Beta strand

467 – 471

5

Beta strand

474 – 479

6

Helix

484 – 486

3

Helix

487 – 499

13

Helix

505 – 510

6

Beta strand

518 – 520

3

Beta strand

523 – 525

3

Helix

531 – 540

10

Beta strand

544 – 546

3

Beta strand

554 – 558

5

Beta strand

564 – 568

5

Beta strand

576 – 579

4

Sequences

	Sequence		Length	Mass (Da)
	P18956-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 772F652EBA2A5F00	FASTA	580	61,768
	10 20 30 40 50 60 MIKPTFLRRV AIAALLSGSC FSAAAAPPAP PVSYGVEEDV FHPVRAKQGM VASVDATATQ 70 80 90 100 110 120 VGVDILKEGG NAVDAAVAVG YALAVTHPQA GNLGGGGFML IRSKNGNTTA IDFREMAPAK 130 140 150 160 170 180 ATRDMFLDDQ GNPDSKKSLT SHLASGTPGT VAGFSLALDK YGTMPLNKVV QPAFKLARDG 190 200 210 220 230 240 FIVNDALADD LKTYGSEVLP NHENSKAIFW KEGEPLKKGD TLVQANLAKS LEMIAENGPD 250 260 270 280 290 300 EFYKGTIAEQ IAQEMQKNGG LITKEDLAAY KAVERTPISG DYRGYQVYSM PPPSSGGIHI 310 320 330 340 350 360 VQILNILENF DMKKYGFGSA DAMQIMAEAE KYAYADRSEY LGDPDFVKVP WQALTNKAYA 370 380 390 400 410 420 KSIADQIDIN KAKPSSEIRP GKLAPYESNQ TTHYSVVDKD GNAVAVTYTL NTTFGTGIVA 430 440 450 460 470 480 GESGILLNNQ MDDFSAKPGV PNVYGLVGGD ANAVGPNKRP LSSMSPTIVV KDGKTWLVTG 490 500 510 520 530 540 SPGGSRIITT VLQMVVNSID YGLNVAEATN APRFHHQWLP DELRVEKGFS PDTLKLLEAK 550 560 570 580 GQKVALKEAM GSTQSIMVGP DGELYGASDP RSVDDLTAGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt." Suzuki H., Kumagai H., Echigo T., Tochikura T. J. Bacteriol. 171:5169-5172(1989) [PubMed: 2570061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-41 AND 391-403. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-362. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Escherichia coli gamma-glutamyltranspeptidase mutants deficient in processing to subunits." Hashimoto W., Suzuki H., Nohara S., Kumagai H. Biochem. Biophys. Res. Commun. 189:173-178(1992) [PubMed: 1360205] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M28722 Genomic DNA. Translation: AAA23869.1.
U18997 Genomic DNA. Translation: AAA58245.1.
U00096 Genomic DNA. Translation: AAC76472.1.
AP009048 Genomic DNA. Translation: BAE77846.1.
U00039 Genomic DNA. Translation: AAB18422.1.

PIR

EKECEX. JV0028.

RefSeq

AP_004345.1.
NP_417904.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DBU	X-ray	1.95	A/C	25-390	[»]
			B/D	391-580	[»]
2DBW	X-ray	1.80	A/C	25-390	[»]
			B/D	391-580	[»]
2DBX	X-ray	1.70	A/C	25-390	[»]
			B/D	391-580	[»]
2DG5	X-ray	1.60	A/C	25-390	[»]
			B/D	391-580	[»]
2E0W	X-ray	2.55	A/B	25-580	[»]
2E0X	X-ray	1.95	A/C	25-390	[»]
			B/D	391-580	[»]
2E0Y	X-ray	2.02	A/C	25-390	[»]
			B/D	391-580	[»]
2Z8I	X-ray	1.65	A/C	25-390	[»]
			B/D	391-580	[»]
2Z8J	X-ray	2.05	A/C	25-390	[»]
			B/D	391-580	[»]
2Z8K	X-ray	1.65	A/C	25-390	[»]
			B/D	391-580	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9758N.

STRING

P18956.

Protein family/group databases

MEROPS

T03.001.

Genome annotation databases

GeneID

947947.

GenomeReviews

Gene locus JW3412 in contig AP009048_GR.
Gene locus b3447 in contig U00096_GR.

KEGG

ecj:JW3412.
eco:b3447.

Organism-specific databases

EchoBASE

EB0369.

EcoGene

EG10374. ggt.

CMR

Search...

Phylogenomic databases

eggNOG

COG0405.

HOGENOM

HBG738311.

OMA

FMLVHLA.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10374-MONOMER.
ECOL168927:B3447-MONOMER.

Gene expression databases

Genevestigator

P18956.

Family and domain databases

InterPro

IPR000101. GGT_peptidase.
[Graphical view]

PANTHER

PTHR11686. GGT_peptidase. 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. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01212. Ceftriaxone.

Entry information

Entry name

GGT_ECOLI

Accession

Primary (citable) accession number: P18956
Secondary accession number(s): Q2M7B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	February 9, 2010
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)