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P14916

- URE23_HELPY

UniProt

P14916 - URE23_HELPY

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Protein

Urease subunit alpha

Gene

ureA

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach.1 Publication

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.2 PublicationsUniRule annotation

Kineticsi

  1. KM=0.48 mM for urea1 Publication

Vmax=1.1 mmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.0. Active from pH 4.0 to 10.0. In unbuffered solutions, the dodecameric complex is active at pH 3.0.2 Publications

Pathwayi

GO - Molecular functioni

  1. nickel cation binding Source: InterPro
  2. urease activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
  2. urea catabolic process Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciHPY:HP0073-MONOMER.
UniPathwayiUPA00258; UER00370.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit alphaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit alphaUniRule annotation
Gene namesi
Name:ureAUniRule annotation
Synonyms:hpuA
Ordered Locus Names:HP_0073
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000429: Chromosome

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation
Note: Also associates with the outer membrane upon autolysis of neighboring bacteria.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells do not express urease.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Urease subunit alphaPRO_0000098075Add
BLAST

Proteomic databases

PRIDEiP14916.

Expressioni

Inductioni

By nickel ions.1 Publication

Interactioni

Subunit structurei

Heterohexamer of 3 UreA (alpha) and 3 UreB (beta) subunits. Four heterohexamers assemble to form a 16 nm dodecameric complex.1 PublicationUniRule annotation

Protein-protein interaction databases

DIPiDIP-3146N.
IntActiP14916. 6 interactions.
MINTiMINT-180633.
STRINGi85962.HP0073.

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2521Combined sources
Helixi32 – 4918Combined sources
Helixi54 – 607Combined sources
Helixi61 – 633Combined sources
Turni67 – 693Combined sources
Helixi74 – 774Combined sources
Beta strandi80 – 878Combined sources
Beta strandi90 – 978Combined sources
Beta strandi117 – 1193Combined sources
Turni120 – 1234Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi139 – 1424Combined sources
Helixi147 – 1493Combined sources
Beta strandi154 – 1563Combined sources
Helixi158 – 1614Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi173 – 1764Combined sources
Beta strandi181 – 1888Combined sources
Helixi208 – 22114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E9YX-ray3.00A1-238[»]
1E9ZX-ray3.00A1-238[»]
ProteinModelPortaliP14916.
SMRiP14916. Positions 1-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14916.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 102102Urease gammaAdd
BLAST
Regioni103 – 238136Urease betaAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the urease gamma subunit family.UniRule annotation
In the C-terminal section; belongs to the urease beta subunit family.UniRule annotation

Phylogenomic databases

KOiK14048.
OMAiFAHEEER.
OrthoDBiEOG69PQ9G.

Family and domain databases

Gene3Di2.10.150.10. 1 hit.
3.30.280.10. 1 hit.
HAMAPiMF_01954. Urease_beta.
MF_01955. Urease_beta_gamma.
InterProiIPR002019. Urease_beta.
IPR008223. Urease_gamma-beta_su.
IPR002026. Urease_gamma/gamma-beta_su.
[Graphical view]
PfamiPF00699. Urease_beta. 1 hit.
PF00547. Urease_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF001225. Urease_gammabeta. 1 hit.
ProDomiPD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51278. SSF51278. 1 hit.
SSF54111. SSF54111. 1 hit.
TIGRFAMsiTIGR00192. urease_beta. 1 hit.
TIGR00193. urease_gam. 1 hit.

Sequencei

Sequence statusi: Complete.

P14916-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLTPKELDK LMLHYAGELA KKRKEKGIKL NYVEAVALIS AHIMEEARAG
60 70 80 90 100
KKTAAELMQE GRTLLKPDDV MDGVASMIHE VGIEAMFPDG TKLVTVHTPI
110 120 130 140 150
EANGKLVPGE LFLKNEDITI NEGKKAVSVK VKNVGDRPVQ IGSHFHFFEV
160 170 180 190 200
NRCLDFDREK TFGKRLDIAS GTAVRFEPGE EKSVELIDIG GNRRIFGFNA
210 220 230
LVDRQADNES KKIALHRAKE RGFHGAKSDD NYVKTIKE
Length:238
Mass (Da):26,540
Last modified:May 1, 1992 - v2
Checksum:i4E77328669CD9A2D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141H → S AA sequence (PubMed:2318539)Curated
Sequence conflicti37 – 371A → R in CAA34932. (PubMed:2326167)Curated
Sequence conflicti49 – 491A → R in CAA34932. (PubMed:2326167)Curated
Sequence conflicti132 – 1332KN → PP in CAA34932. (PubMed:2326167)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17079 Genomic DNA. Translation: CAA34932.1.
M60398 Genomic DNA. Translation: AAA25020.1.
AB032429 Genomic DNA. Translation: BAA84532.1.
AE000511 Genomic DNA. Translation: AAD07144.1.
PIRiA38537. URKCAP.
RefSeqiNP_206873.1. NC_000915.1.
WP_000779223.1. NC_018939.1.
YP_006933995.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD07144; AAD07144; HP_0073.
GeneIDi13869249.
900171.
KEGGiheo:C694_00355.
hpy:HP0073.
PATRICi20591349. VBIHelPyl33062_0076.

Cross-referencesi

Web resourcesi

Protein Spotlight

Going unnoticed - Issue 95 of June 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17079 Genomic DNA. Translation: CAA34932.1 .
M60398 Genomic DNA. Translation: AAA25020.1 .
AB032429 Genomic DNA. Translation: BAA84532.1 .
AE000511 Genomic DNA. Translation: AAD07144.1 .
PIRi A38537. URKCAP.
RefSeqi NP_206873.1. NC_000915.1.
WP_000779223.1. NC_018939.1.
YP_006933995.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E9Y X-ray 3.00 A 1-238 [» ]
1E9Z X-ray 3.00 A 1-238 [» ]
ProteinModelPortali P14916.
SMRi P14916. Positions 1-238.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-3146N.
IntActi P14916. 6 interactions.
MINTi MINT-180633.
STRINGi 85962.HP0073.

Proteomic databases

PRIDEi P14916.

Protocols and materials databases

DNASUi 900171.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD07144 ; AAD07144 ; HP_0073 .
GeneIDi 13869249.
900171.
KEGGi heo:C694_00355.
hpy:HP0073.
PATRICi 20591349. VBIHelPyl33062_0076.

Phylogenomic databases

KOi K14048.
OMAi FAHEEER.
OrthoDBi EOG69PQ9G.

Enzyme and pathway databases

UniPathwayi UPA00258 ; UER00370 .
BioCyci HPY:HP0073-MONOMER.

Miscellaneous databases

EvolutionaryTracei P14916.

Family and domain databases

Gene3Di 2.10.150.10. 1 hit.
3.30.280.10. 1 hit.
HAMAPi MF_01954. Urease_beta.
MF_01955. Urease_beta_gamma.
InterProi IPR002019. Urease_beta.
IPR008223. Urease_gamma-beta_su.
IPR002026. Urease_gamma/gamma-beta_su.
[Graphical view ]
Pfami PF00699. Urease_beta. 1 hit.
PF00547. Urease_gamma. 1 hit.
[Graphical view ]
PIRSFi PIRSF001225. Urease_gammabeta. 1 hit.
ProDomi PD002319. Urease_gamma_reg. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF51278. SSF51278. 1 hit.
SSF54111. SSF54111. 1 hit.
TIGRFAMsi TIGR00192. urease_beta. 1 hit.
TIGR00193. urease_gam. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiURE23_HELPY
AccessioniPrimary (citable) accession number: P14916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 1, 1992
Last modified: November 26, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3