Urease subunit alpha - Helicobacter pylori

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Reviewed, UniProtKB/Swiss-Prot P14916 (URE23_HELPY)

Last modified February 9, 2010. Version 95. History...

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

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Names and origin

Protein names

Recommended 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

Organism

Helicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]

Taxonomic identifier

210 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

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Protein attributes

Sequence length	238 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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 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. HAMAP MF_01955
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: K_M=0.48 mM for urea HAMAP MF_01955 V_max=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.

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Ontologies

Keywords
Biological process	Virulence
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW urea metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nickel ion binding Inferred from electronic annotation. Source: InterPro urease activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 238

238

Urease subunit alpha HAMAP MF_01955

PRO_0000098075

Regions

Region

1 – 102

102

Urease gamma HAMAP MF_01955

Region

103 – 238

136

Urease beta HAMAP MF_01955

Experimental info

Sequence conflict

H → S AA sequence Ref.5

Sequence conflict

A → R in CAA34932. Ref.1

Sequence conflict

A → R in CAA34932. Ref.1

Sequence conflict

132 – 133

KN → PP in CAA34932. Ref.1

Secondary structure

238

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P14916-1 [UniParc].

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

FASTA

238

26,540

        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

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References

	« Hide 'large scale' referencesShow '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. 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: 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: 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.

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Web resources

Protein Spotlight

Going unnoticed - Issue 95 of June 2008

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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.

PIR

URKCAP. A38537.

RefSeq

NP_206873.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E9Y	X-ray	3.00	A	1-238	[»]
1E9Z	X-ray	3.00	A	1-238	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3146N.

Genome annotation databases

GeneID

900171.

GenomeReviews

Gene locus HP_0073 in contig AE000511_GR.

KEGG

hpy:HP0073.

NMPDR

fig|85962.1.peg.71.

TIGR

HP_0073.

Phylogenomic databases

HOGENOM

HBG365918.

OMA

VHHPIRG.

Enzyme and pathway databases

BRENDA

3.5.1.5. 1131.

Family and domain databases

HAMAP

MF_01955. Urease_beta_gamma.
[Tree]

InterPro

IPR002026. Urease_alpha/gamma.
IPR002019. Urease_beta.
IPR008223. Urease_gammabeta.
[Graphical view]

Gene3D

G3DSA:2.10.150.10. Urease_beta. 1 hit.
G3DSA:3.30.280.10. Urease_gamma_reg. 1 hit.

Pfam

PF00699. Urease_beta. 1 hit.
PF00547. Urease_gamma. 1 hit.
[Graphical view]

PIRSF

PIRSF001225. Urease_gammabeta. 1 hit.

ProDom

PD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00192. urease_beta. 1 hit.
TIGR00193. urease_gam. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

URE23_HELPY

Accession

Primary (citable) accession number: P14916

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	May 1, 1992
Last modified:	February 9, 2010
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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