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Reviewed, UniProtKB/Swiss-Prot P69996 (URE1_HELPY)

Last modified November 25, 2008. Version 41. 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 beta
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit beta
Gene names
Name: ureB
Synonyms: hpuB
Ordered Locus Names: HP_0072
OrganismHelicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]
Taxonomic identifier210 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length569 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).

Cofactor

Binds 2 nickel ions per subunit.

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.

Post-translational modification

Carbamylation allows a single lysine to coordinate two 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

Belongs to the urease family.

Contains 1 urease domain.

Caution

The orthologous protein is known as the alpha subunit (ureC) 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 pH3.0.

Ontologies

Keywords

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

Gene Ontology (GO)

   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

urea metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: HAMAP

   Molecular functionnickel ion binding

Inferred from electronic annotation. Source: InterPro

urease activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 569569Urease subunit beta
PRO_0000067533

Regions

Domain131 – 569439Urease

Sites

Active site3221Proton donor Probable
Metal binding1361Nickel 2
Metal binding1381Nickel 2
Metal binding2191Nickel 1; via carbamate group
Metal binding2191Nickel 2; via carbamate group
Metal binding2481Nickel 1
Metal binding2741Nickel 1
Metal binding3621Nickel 2
Binding site2211Substrate Probable

Amino acid modifications

Modified residue2191N6-carboxylysine

Experimental info

Sequence conflict101V → A in CAA34933. Ref.2
Sequence conflict191D → A Ref.2
Sequence conflict221R → C AA sequence Ref.4
Sequence conflict271D → C AA sequence Ref.4
Sequence conflict1041M → T in CAA34933. Ref.2
Sequence conflict1811W → F in CAA34933. Ref.2
Sequence conflict1931L → F in CAA34933. Ref.2
Sequence conflict2181F → L in CAA34933. Ref.2
Sequence conflict2731F → Y in CAA34933. Ref.2
Sequence conflict5401P → S in CAA34933. Ref.2
Sequence conflict554 – 56916SKPAN…LFSIF → LNQPIK in CAA34933. Ref.2

Secondary structure

................................................................................................................. 569
Helix Strand Turn

Details...

Sequences

Sequence