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Q2YPD5 (URE11_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Urease subunit alpha 1
EC=3.5.1.5
Alternative name(s):
Urea amidohydrolase subunit alpha 1
Gene names
Name:ureC1
Ordered Locus Names:BAB1_0300
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella ›

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May protect brucellae during their passage through the stomach. The major route of infection in human brucellosis is oral. Ref.1

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP-Rule 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-Rule MF_01953

Subunit structure

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions By similarity. HAMAP-Rule MF_01953

Disruption phenotype

Disruption of the ure1 gene cluster via a large in-frame deletion in this gene abrogates urease activity. Ref.1

Sequence similarities

Belongs to the urease family.

Contains 1 urease domain.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

urea catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnickel cation binding

Inferred from electronic annotation. Source: HAMAP

urease activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 570570Urease subunit alpha 1 HAMAP-Rule MF_01953
PRO_0000234141

Regions

Domain131 – 570440Urease

Sites

Active site3221Proton donor By similarity
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
Metal binding3621Nickel 2 By similarity
Binding site2211Substrate By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YPD5 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 648464AD7EDBB7EC

FASTA57061,011
        10         20         30         40         50         60 
MPARISRATY AQMFGPTVGD KVRLADTDLI IEVERDLTTY GEEVKFGGGK VIRDGMGQSQ 

        70         80         90        100        110        120 
LSRAEGAMDT VITNALILDH SGIYKADIGL LDGRIALIGK AGNPDTQPGI SIIIGPGTEI 

       130        140        150        160        170        180 
IAGEGKIVTA GGIDTHVHFI SPQQVDEALN AGITCMVGGG TGPAHGTLAT TCTPGPWHIA 

       190        200        210        220        230        240 
RLIQSFDGLP MNIGVFGKGN ASLPGALEEM VRAGACGLKL HEDWGCTPAA IDNCLSVADH 

       250        260        270        280        290        300 
FDVQVAIHTD TLNEGGFVED TLNAFKGRTI HSFHTEGAGG GHAPDIIRVC QYPNVLPAST 

       310        320        330        340        350        360 
NPTRPYTVNT IAEHLDMLMV CHHLSPAIPE DIAFAESRIR KETIAAEDIL HDMGAFSIIS 

       370        380        390        400        410        420 
SDSQAMGRVG EMIIRCWQTA DKMKKQRGSL PDDRPGNDNY RARRYIAKYT INPAIAHGMA 

       430        440        450        460        470        480 
HEIGSVEVGK RADLVLWNPA FFGVKPDMVL LGGWIATAPM GDANGSIPTP QPMHTRPMFG 

       490        500        510        520        530        540 
SFGKALTNTS ITFVSQAAMD EGLREKIGVD KQLVAVVNTR GGIGKHSMIL NNAMPQMEVD 

       550        560        570 
PETYEVRADG ELLTCEPVDV VPMAQRYFLF

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the urease operon of Brucella abortus and assessment of its role in virulence of the bacterium."
Sangari F.J., Seoane A., Rodriguez M.C., Aguero J., Garcia Lobo J.M.
Infect. Immun. 75:774-780(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, CHARACTERIZATION OF ROLE IN VIRULENCE.
[2]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF361941 Genomic DNA. Translation: AAK51069.1.
AM040264 Genomic DNA. Translation: CAJ10256.1.
RefSeqYP_413771.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YPD5.
SMRQ2YPD5. Positions 3-570.
ModBaseSearch...

Protein-protein interaction databases

STRING359391.BAB1_0300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ10256; CAJ10256; BAB1_0300.
GeneID3789048.
KEGGbmf:BAB1_0300.
PATRIC17843468. VBIBruMel86222_0320.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0804.
HOGENOMHOG000075064.
KOK01428.
OMATIHAFHT.
ProtClustDBPRK13207.

Enzyme and pathway databases

BioCycBMEL359391:GJOQ-306-MONOMER.
UniPathwayUPA00258; UER00370.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
InterProIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
IPR011612. Urease_alpha_N.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR017950. Urease_asu_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
SUPFAMSSF51338. Metalo_hydrolase. 2 hits.
TIGRFAMsTIGR01792. urease_alph. 1 hit.
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameURE11_BRUA2
AccessionPrimary (citable) accession number: Q2YPD5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: February 7, 2006
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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