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Reviewed, UniProtKB/Swiss-Prot Q5FB23 (URE1_CAMLA)

Last modified February 9, 2010. Version 34. 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

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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
OrganismCampylobacter lari
Taxonomic identifier201 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

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Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953

Cofactor

Binds 2 nickel ions per subunit By similarity. HAMAP MF_01953

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. HAMAP MF_01953

Subcellular location

Cytoplasm By similarity HAMAP MF_01953.

Post-translational modification

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

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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 565565Urease subunit beta HAMAP MF_01953
PRO_0000234287

Regions

Domain130 – 565436Urease

Sites

Active site3211Proton donor By similarity
Metal binding1351Nickel 2 By similarity
Metal binding1371Nickel 2 By similarity
Metal binding2181Nickel 1; via carbamate group By similarity
Metal binding2181Nickel 2; via carbamate group By similarity
Metal binding2471Nickel 1 By similarity
Metal binding2731Nickel 1 By similarity
Metal binding3611Nickel 2 By similarity
Binding site2201Substrate By similarity

Amino acid modifications

Modified residue2181N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5FB23-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 5F5E0D54E0282B27

FASTA56561,439
        10         20         30         40         50         60 
MIKISKKDYV NMYGPTTNDR VRLADTDLIL RVEKDYTLYG EEVKFGGGKN IRDGMAQSVS 

        70         80         90        100        110        120 
EGDFPDLVLT NALIVDYTGI YKADIGIKNG YIVGIGKAGN PDIQDGVDPS LIIGTNTDII 

       130        140        150        160        170        180 
GAEGLIVTAG GIDTHIHFIS PTQIECALYS GVTTMIGGGI GPSEGTNATT CTSGAYHIHS 

       190        200        210        220        230        240 
MLKATQNYPM NFGFLGKGNS SNKNALKEQI IAGACGLKIH EDWGATSSVI DASLNIADEM 

       250        260        270        280        290        300 
DIQVAIHTDT LNEAGFVEDT IKAINGRVIH TFHTEGAGGG HAPDIIKMAG FENVLPASTN 

       310        320        330        340        350        360 
PTMPFTKNTI DEHLDMLMVC HHLDNKIKED VEFADSRIRP ETIAAEDKLH DMGVFSIMSS 

       370        380        390        400        410        420 
DSQAMGRVGE VILRTWQSAD KCKKEFGALK EDNDLDDNFR IKRYIAKYTI NPAIAHGIDS 

       430        440        450        460        470        480 
YVGSIEVGKF ADLVLWQPKF FGVKPKLILK GGLIVGAKIG DANASIPTPE PIIYEKMFGA 

       490        500        510        520        530        540 
NLNENALHFV SKASLDANIP EKLSLKRKCV AVKNCRNITK KDLKFNDKVQ DIEVNPQTYE 

       550        560 
VKINGELISS KSVDSLALAR KYFMI

« Hide

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References

[1]"Genetic heterogeneity of urease gene loci in urease-positive thermophilic Campylobacter (UPTC)."
Usui K., Iida H., Ueno H., Sekizuka T., Matsuda M., Murayama O., Cherie Millar B., Moore J.E.
Int. J. Hyg. Environ. Health 209:541-545(2006) [PubMed: 16798085] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CF89-12.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB201709 Genomic DNA. Translation: BAD89502.1.

3D structure databases

SMRQ5FB23. Positions 1-562.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.5.1.5. 290636.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
IPR011612. Urease_alpha_N.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR017952. Urease_asu_core.
IPR017950. Urease_asu_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
TIGRFAMsTIGR01792. urease_alph. 1 hit.
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameURE1_CAMLA
AccessionPrimary (citable) accession number: Q5FB23
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 15, 2005
Last modified: February 9, 2010
This is version 34 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)

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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