O25743 (O25743_HELPY) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Gamma-glutamyltranspeptidase (Ggt) EMBL AAD08162.1

Gene names

Ordered Locus Names:

HP_1118

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Technical term	3D-structure PDB 2NQO PDB 3FNM PDB 2QMC PDB 2QM6 Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	gamma-glutamyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	O25743 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 9A5B4E06B6B8967F	FASTA	567	61,151
	10 20 30 40 50 60 MRRSFLKTIG LGVIALFLGL LNPLSAASYP PIKNTKVGLA LSSHPLASEI GQKVLEEGGN 70 80 90 100 110 120 AIDAAVAIGF ALAVVHPAAG NIGGGGFAVI HLANGENVAL DFREKAPLKA TKNMFLDKQG 130 140 150 160 170 180 NVVPKLSEDG YLAAGVPGTV AGMEAMLKKY GTKKLSQLID PAIKLAENGY AISQRQAETL 190 200 210 220 230 240 KEARERFLKY SSSKKYFFKK GHLDYQEGDL FVQKDLAKTL NQIKTLGAKG FYQGQVAELI 250 260 270 280 290 300 EKDMKKNGGI ITKEDLASYN VKWRKPVVGS YRGYKIISMS PPSSGGTHLI QILNVMENAD 310 320 330 340 350 360 LSALGYGASK NIHIAAEAMR QAYADRSVYM GDADFVSVPV DKLINKAYAK KIFDTIQPDT 370 380 390 400 410 420 VTPSSQIKPG MGQLHEGSNT THYSVADRWG NAVSVTYTIN ASYGSAASID GAGFLLNNEM 430 440 450 460 470 480 DDFSIKPGNP NLYGLVGGDA NAIEANKRPL SSMSPTIVLK NNKVFLVVGS PGGSRIITTV 490 500 510 520 530 540 LQVISNVIDY NMNISEAVSA PRFHMQWLPD ELRIEKFGMP ADVKDNLTKM GYQIVTKPVM 550 560 GDVNAIQVLP KTKGSVFYGS TDPRKEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.
[2]	"Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis." Morrow A.L., Williams K., Sand A., Boanca G., Barycki J.J. Biochemistry 46:13407-13414(2007) [PubMed: 17960917] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 25-379 AND 381-567.
[3]	"Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad." Boanca G., Sand A., Okada T., Suzuki H., Kumagai H., Fukuyama K., Barycki J.J. J. Biol. Chem. 282:534-541(2007) [PubMed: 17107958] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 27-379 AND 380-567.
[4]	"Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis." Williams K., Cullati S., Sand A., Biterova E.I., Barycki J.J. Biochemistry 48:2459-2467(2009) [PubMed: 19256527] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 25-379 AND 380-567.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000511 Genomic DNA. Translation: AAD08162.1.

PIR

F64659.

RefSeq

NP_207909.1. NC_000915.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NQO	X-ray	1.90	A/C	27-379	[»]
			B/D	380-567	[»]
2QM6	X-ray	1.60	A/C	25-379	[»]
			B/D	380-567	[»]
2QMC	X-ray	1.55	A/C	25-379	[»]
			B/D	381-567	[»]
3FNM	X-ray	1.70	A/C	25-379	[»]
			B/D	380-567	[»]

ProteinModelPortal

O25743.

SMR

O25743. Positions 31-565.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3652N.

MINT

MINT-160568.

Protein family/group databases

MEROPS

T03.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

899655.

GenomeReviews

Gene locus HP_1118 in contig AE000511_GR.

KEGG

hpy:HP1118.

NMPDR

fig|85962.1.peg.1105.

PATRIC

20593579. VBIHelPyl33062_1169.

TIGR

HP_1118.

Phylogenomic databases

HOGENOM

HBG738311.

OMA

ANNITRT.

ProtClustDB

CLSK872502.

Family and domain databases

InterPro

IPR000101. GGT_peptidase.
[Graphical view]

KO

K00681.

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...

Entry information

Entry name

O25743_HELPY

Accession

Primary (citable) accession number: O25743

Entry history

Integrated into UniProtKB/TrEMBL:	January 1, 1998
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)