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P14916 (URE23_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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 (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
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. Ref.10

Catalytic activity

Urea + H2O = CO2 + 2 NH3. Ref.6 Ref.9

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP-Rule MF_01955

Subunit structure

Heterohexamer of 3 UreA (alpha) and 3 UreB (beta) subunits. Four heterohexamers assemble to form a 16 nm dodecameric complex. Ref.14

Subcellular location

Cytoplasm. Note: Also associates with the outer membrane upon autolysis of neighboring bacteria. Ref.11

Induction

By nickel ions. Ref.12

Disruption phenotype

Cells do not express urease. Ref.8

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.

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 Ref.6

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
Reference proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

urea catabolic process

Inferred from mutant phenotype Ref.8. Source: CACAO

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnickel cation binding

Inferred from electronic annotation. Source: InterPro

urease activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238Urease subunit alpha HAMAP-Rule MF_01955
PRO_0000098075

Regions

Region1 – 102102Urease gamma HAMAP-Rule MF_01955
Region103 – 238136Urease beta HAMAP-Rule MF_01955

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT STRUCTURE, PH DEPENDENCE.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Going unnoticed - Issue 95 of June 2008

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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. NC_000915.1.
YP_006933995.1. NC_018939.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E9YX-ray3.00A1-238[»]
1E9ZX-ray3.00A1-238[»]
ProteinModelPortalP14916.
SMRP14916. Positions 1-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-3146N.
IntActP14916. 5 interactions.
MINTMINT-180633.
STRING85962.HP0073.

Proteomic databases

PRIDEP14916.

Protocols and materials databases

DNASU900171.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD07144; AAD07144; HP_0073.
GeneID13869249.
900171.
KEGGheo:C694_00355.
hpy:HP0073.
PATRIC20591349. VBIHelPyl33062_0076.

Phylogenomic databases

KOK14048.
OMAFAHEEER.
OrthoDBEOG69PQ9G.
ProtClustDBPRK13986.

Enzyme and pathway databases

BioCycHPY:HP0073-MONOMER.
UniPathwayUPA00258; UER00370.

Family and domain databases

Gene3D2.10.150.10. 1 hit.
3.30.280.10. 1 hit.
HAMAPMF_01954. Urease_beta.
MF_01955. Urease_beta_gamma.
InterProIPR002019. Urease_beta.
IPR008223. Urease_gamma-beta_su.
IPR002026. Urease_gamma/gamma-beta_su.
[Graphical view]
PfamPF00699. Urease_beta. 1 hit.
PF00547. Urease_gamma. 1 hit.
[Graphical view]
PIRSFPIRSF001225. Urease_gammabeta. 1 hit.
ProDomPD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF51278. SSF51278. 1 hit.
SSF54111. SSF54111. 1 hit.
TIGRFAMsTIGR00192. urease_beta. 1 hit.
TIGR00193. urease_gam. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP14916.

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: February 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names