Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P50045 (URE1_HELMU)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 · Cross-references · Entry information · Relevant documents

Hide | Top

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
OrganismHelicobacter mustelae
Taxonomic identifier217 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Hide | Top

Protein attributes

Sequence length308 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953

Cofactor

Binds 2 nickel ions per subunit By similarity.

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953

Subunit structure

Heterohexamer of 3 ureA (alpha) and 3 ureB (beta) subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions By similarity.

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.

Hide | Top

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processurea metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnickel ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

urease activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›308›308Urease subunit beta HAMAP MF_01953
PRO_0000067532

Regions

Domain131 – ›308›178Urease

Sites

Metal binding1361Nickel 2 By similarity
Metal binding1381Nickel 2 By similarity
Metal binding2191Nickel 1; via carbamate group By similarity
Metal binding2191Nickel 2; via carbamate group By similarity
Metal binding2481Nickel 1 By similarity
Metal binding2741Nickel 1 By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Experimental info

Non-terminal residue3081

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P50045-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1F11F29A5B3C84B1

FASTA30832,118
        10         20         30         40         50         60 
MIKISRKEYV SMYGPTTGDK VRLGDTELIA EIEKDYTVYG EEIKFGGGKT IRDGMSQSVS 

        70         80         90        100        110        120 
PDVNELDAVI TNAMIIDYTG IYKADIGIKD GKIAGIGKAG NRDTQDGVGM DLVVGASTEA 

       130        140        150        160        170        180 
IAGEGLIVTA GGIDTHIHFI SPTQIPTALY SGVTTMIGGG TGPAAGTFAT TISPGEWNIK 

       190        200        210        220        230        240 
QMIRAAEEYT MNLGFFGKGN TSNVKALEDQ IKAGALGFKV HEDCGSTPAV INHSLDIAEK 

       250        260        270        280        290        300 
YDVQVAIHTD TLNEGGAVED TLAAIGGRTI HTFHTEGAGG GHAPDIIKAA GEANILPAST 


NPTIPFTK

« Hide

Hide | Top

References

[1]"Construction and characterization of an isogenic urease-negative mutant of Helicobacter mustelae."
Solnick J.V., Josenhans C., Tompkins L.S., Labigne A.
Infect. Immun. 63:3718-3721(1995) [PubMed: 7642313] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NCTC 12032.

Hide | Top

Cross-references

Sequence databases

L33462 Genomic DNA. Translation: AAC41484.1.

3D structure databases

HSSPHSSP built from PDB template 1E9Z based on UniProtKB P14917.
SMRP50045. Positions 1-307.
ModBaseSearch...

Protein family/group databases

MEROPSM38.982.

Enzyme and pathway databases

BRENDA3.5.1.5. 141617.

Family and domain databases

HAMAPMF_01953.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR011612. Urease_alpha_N.
IPR017951. Urease_asu_c.
IPR017950. Urease_asu_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. Partial match.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameURE1_HELMU
AccessionPrimary (citable) accession number: P50045
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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