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Reviewed, UniProtKB/Swiss-Prot P14916 (URE23_HELPY)

Last modified September 2, 2008. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Urease subunit alpha
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit alpha
Gene names
Name: ureA
Synonyms: hpuA
Ordered Locus Names: HP_0073
OrganismHelicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]
Taxonomic identifier210 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach.

Catalytic activity

Urea + H(2)O = CO(2) + 2 NH(3).

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.

Subunit structure

Heterohexamer of 3 ureA (alpha) and 3 ureB (beta) subunits. Four heterohexamers assemble to form a 16 nm dodecameric complex.

Subcellular location

Cytoplasm. Note= Also associates with the outer membrane upon autolysis of neighboring bacteria.

Induction

By nickel ions.

Miscellaneous

The novel dodecameric structure of the enzyme may allow it to remain active at the cell surface at acidic gastric pH. Within this dodecameric structure the 12 active sites are clustered within the interior of the proteinaceous shell. This may allow a high local concentration of ammonia within the enzyme which may protect the nickel-chelating groups from protonation.

Strains lacking this gene do not express urease.

Sequence similarities

In the N-terminal section; belongs to the urease gamma subunit family.

In the C-terminal section; belongs to the urease beta subunit family.

Caution

The orthologous protein is known as the gamma/beta subunit (ureAB) in most other bacteria.

Biophysicochemical properties

Kinetic parameters:

KM=0.48 mM for urea

Vmax=1.1 mmol/min/mg enzyme

pH dependence:

Optimum pH is 8.0. Active from pH 4.0 to 10.0. In unbuffered solutions, the dodecameric complex is active at pH 3.0.

Ontologies

Keywords

   Biological processVirulence
   Cellular componentCytoplasm
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing

Gene Ontology (GO)

   Biological processurea metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: HAMAP

   Molecular functionurease activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 238238Urease subunit alpha

Regions

Region1 – 102102Urease gamma
Region103 – 238136Urease beta

Experimental info

Sequence conflict141H → S AA sequence Ref.5
Sequence conflict371A → R in CAA34932. Ref.1
Sequence conflict491A → R in CAA34932. Ref.1
Sequence conflict132 – 1332KN → PP in CAA34932. Ref.1

Secondary structure

....................................... 238
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14916-1 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: 4E77328669CD9A2D

FASTA23826,540
        10         20         30         40         50         60 
MKLTPKELDK LMLHYAGELA KKRKEKGIKL NYVEAVALIS AHIMEEARAG KKTAAELMQE 

        70         80         90        100        110        120 
GRTLLKPDDV MDGVASMIHE VGIEAMFPDG TKLVTVHTPI EANGKLVPGE LFLKNEDITI 

       130        140        150        160        170        180 
NEGKKAVSVK VKNVGDRPVQ IGSHFHFFEV NRCLDFDREK TFGKRLDIAS GTAVRFEPGE 

       190        200        210        220        230 
EKSVELIDIG GNRRIFGFNA LVDRQADNES KKIALHRAKE RGFHGAKSDD NYVKTIKE 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of two genes from Helicobacter pylori encoding for urease subunits."
Clayton C.L., Pallen M.J., Kleanthous H., Wren B.W., Tabaqchali S.
Nucleic Acids Res. 18:362-362(1990) [PubMed: 2326167] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CPM630.
[2]"Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity."
Labigne A., Cussac V., Courcoux P.
J. Bacteriol. 173:1920-1931(1991) [PubMed: 2001995] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 85P.
[3]"Identification of the urease operon in Helicobacter pylori and its control by mRNA decay in response to pH."
Akada J.K., Shirai M., Takeuchi H., Tsuda M., Nakazawa T.
Mol. Microbiol. 36:1071-1084(2000) [PubMed: 10844692] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: HPK5.
[4]"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. expand/collapse author list , 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.
[5]"Purification and N-terminal analysis of urease from Helicobacter pylori."
Hu L.-T., Mobley H.L.T.
Infect. Immun. 58:992-998(1990) [PubMed: 2318539] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20.
[6]"Purification and characterization of urease from Helicobacter pylori."
Dunn B.E., Campbell G.P., Perez-Perez G.I., Blaser M.J.
J. Biol. Chem. 265:9464-9469(1990) [PubMed: 2188975] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH UREB.
[7]"Purification and characterization of the urease enzymes of Helicobacter species from humans and animals."
Turbett G.R., Hoej P.B., Horne R., Mee B.J.
Infect. Immun. 60:5259-5266(1992) [PubMed: 1452359] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20.
Strain: ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487.
[8]"Expression of Helicobacter pylori urease genes in Escherichia coli grown under nitrogen-limiting conditions."
Cussac V., Ferrero R.L., Labigne A.
J. Bacteriol. 174:2466-2473(1992) [PubMed: 1313413] [Abstract]
Cited for: KNOCKOUT.
Strain: 85P.
[9]"Purification of recombinant Helicobacter pylori urease apoenzyme encoded by ureA and ureB."
Hu L.-T., Foxall P.A., Russell R., Mobley H.L.T.
Infect. Immun. 60:2657-2666(1992) [PubMed: 1612735] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[10]"A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach."
Tsuda M., Karita M., Morshed M.G., Okita K., Nakazawa T.
Infect. Immun. 62:3586-3589(1994) [PubMed: 8039935] [Abstract]
Cited for: FUNCTION.
[11]"Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis."
Phadnis S.H., Parlow M.H., Levy M., Ilver D., Caulkins C.M., Connors J.B., Dunn B.E.
Infect. Immun. 64:905-912(1996) [PubMed: 8641799] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Nickel-responsive induction of urease expression in Helicobacter pylori is mediated at the transcriptional level."
van Vliet A.H.M., Kuipers E.J., Waidner B., Davies B.J., de Vries N., Penn C.W., Vandenbroucke-Grauls C.M.J.E., Kist M., Bereswill S., Kusters J.G.
Infect. Immun. 69:4891-4897(2001) [PubMed: 11447165] [Abstract]
Cited for: INDUCTION.
[13]"Bacterial factors that mediate colonization of the stomach and virulence of Helicobacter pylori."
Clyne M., Dolan B., Reeves E.P.
FEMS Microbiol. Lett. 268:135-143(2007) [PubMed: 17313591] [Abstract]
Cited for: REVIEW ON VIRULENCE OF H.PYLORI.
[14]"Supramolecular assembly and acid resistance of Helicobacter pylori urease."
Ha N.-C., Oh S.-T., Sung J.Y., Cha K.A., Lee M.H., Oh B.-H.
Nat. Struct. Biol. 8:505-509(2001) [PubMed: 11373617] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT STRUCTURE, PH DEPENDENCE.

Web resources

Protein Spotlight

Going unnoticed - Issue 95 of June 2008

Cross-references

Sequence databases

X17079 Genomic DNA. Translation: CAA34932.1.
M60398 Genomic DNA. Translation: AAA25020.1.
AB032429 Genomic DNA. Translation: BAA84532.1.
AE000511 Genomic DNA. Translation: AAD07144.1.
PIRURKCAP. A38537.
RefSeqNP_206873.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1E9YX-ray3.00A1-238[»]
1E9ZX-ray3.00A1-238[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:3146N.

Genome annotation databases

GeneID900171.
GenomeReviewsGene locus HP_0073 in contig AE000511_GR.
KEGGhpy:HP0073.
NMPDRfig|85962.1.peg.71.
TIGRHP_0073.

Phylogenomic databases

HOGENOMP14916.

Family and domain databases

HAMAPMF_01955.
[Tree]
InterProIPR002019. Urease_beta.
IPR002026. Urease_gamma_reg.
IPR008223. Urease_gammabeta.
[Graphical view]
Gene3DG3DSA:2.10.150.10. Urease_beta. 1 hit.
G3DSA:3.30.280.10. Urease_gamma_reg. 1 hit.
PfamPF00699. Urease_beta. 1 hit.
PF00547. Urease_gamma. 1 hit.
[Graphical view]
PIRSFPIRSF001225. Urease_gammabeta. 1 hit.
ProDomPD002326. Urease_beta. 1 hit.
PD002319. Urease_gamma. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00192. urease_beta. 1 hit.
TIGR00193. urease_gam. 1 hit.
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameURE23_HELPY
AccessionPrimary (citable) accession number: P14916
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 1, 1992
Last modified: September 2, 2008
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents