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P18315 (URE2_ENTAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismEnterobacter aerogenes (Aerobacter aerogenes)
Taxonomic identifier548 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Protein attributes

Sequence length106 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Enzyme regulation

The apoenzyme can be activated in vitro in the presence of nickel ions and carbon dioxide, which promotes carbamylation of 'Lys-217' of the UreC (alpha) subunit. Ref.6 Ref.7 Ref.8 Ref.9

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP-Rule MF_01954

Subunit structure

Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme. The apoenzyme interacts with an accessory complex composed of UreD, UreF and UreG, which is required for the assembly of the nickel containing metallocenter of UreC. The UreE protein may also play a direct role as a metallochaperone in nickel transfer to the urease apoprotein. Ref.4 Ref.5 Ref.7 Ref.8 Ref.11

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01954.

Sequence similarities

Belongs to the urease beta subunit family.

Biophysicochemical properties

Kinetic parameters:

KM=2.3 mM for urea Ref.2 Ref.3 Ref.10 Ref.18

Vmax=1.9 mmol/min/mg enzyme

pH dependence:

Optimum pH is 7.75.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processurea catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionurease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 106106Urease subunit beta HAMAP-Rule MF_01954
PRO_0000067577

Experimental info

Mutagenesis391H → A: Reduces activity by 20% and reduces thermal stability above 50 degrees Celsius. Ref.3
Mutagenesis411H → A: Reduces activity by 30% and reduces thermal stability above 50 degrees Celsius. Ref.3

Secondary structure

.................... 106
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18315 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: A232BFCD74864EA6

FASTA10611,695
        10         20         30         40         50         60 
MIPGEYHVKP GQIALNTGRA TCRVVVENHG DRPIQVGSHY HFAEVNPALK FDRQQAAGYR 

        70         80         90        100 
LNIPAGTAVR FEPGQKREVE LVAFAGHRAV FGFRGEVMGP LEVNDE 

« Hide

References

[1]"Sequence of the Klebsiella aerogenes urease genes and evidence for accessory proteins facilitating nickel incorporation."
Mulrooney S.B., Hausinger R.P.
J. Bacteriol. 172:5837-5843(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY.
Strain: CG253.
[2]"Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease."
Martin P.R., Hausinger R.P.
J. Biol. Chem. 267:20024-20027(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[3]"Site-directed mutagenesis of Klebsiella aerogenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding, and catalysis."
Park I.-S., Hausinger R.P.
Protein Sci. 2:1034-1041(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-39 AND HIS-41.
[4]"In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly."
Park I.-S., Carr M.B., Hausinger R.P.
Proc. Natl. Acad. Sci. U.S.A. 91:3233-3237(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREA; UREC AND URED.
[5]"Evidence for the presence of urease apoprotein complexes containing UreD, UreF, and UreG in cells that are competent for in vivo enzyme activation."
Park I.-S., Hausinger R.P.
J. Bacteriol. 177:1947-1951(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREA; UREC; URED; UREF AND UREG.
[6]"Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter."
Park I.-S., Hausinger R.P.
Science 267:1156-1158(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
[7]"Purification and activation properties of UreD-UreF-urease apoprotein complexes."
Moncrief M.B.C., Hausinger R.P.
J. Bacteriol. 178:5417-5421(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREA; UREC; URED AND UREF.
[8]"GTP-dependent activation of urease apoprotein in complex with the UreD, UreF, and UreG accessory proteins."
Soriano A., Hausinger R.P.
Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREA; UREC; URED; UREF AND UREG.
[9]"UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-urease apoprotein complex."
Soriano A., Colpas G.J., Hausinger R.P.
Biochemistry 39:12435-12440(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, ACTIVATION OF THE APOPROTEIN BY UREE.
[10]"Dual effects of ionic strength on Klebsiella aerogenes urease: pH-dependent activation and inhibition."
Mulrooney S.B., Zakharian T., Schaller R.A., Hausinger R.P.
Arch. Biochem. Biophys. 394:280-282(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[11]"Chemical cross-linking and mass spectrometric identification of sites of interaction for UreD, UreF, and urease."
Chang Z., Kuchar J., Hausinger R.P.
J. Biol. Chem. 279:15305-15313(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UREA; UREC; URED AND UREF, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"The crystal structure of urease from Klebsiella aerogenes."
Jabri E., Carr M.B., Hausinger R.P., Karplus P.A.
Science 268:998-1004(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
[13]"Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants."
Jabri E., Karplus P.A.
Biochemistry 35:10616-10626(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
[14]"Characterization of the mononickel metallocenter in H134A mutant urease."
Park I.-S., Michel L.O., Pearson M.A., Jabri E., Karplus P.A., Wang S., Dong J., Scott R.A., Koehler B.P., Johnson M.K., Hausinger R.P.
J. Biol. Chem. 271:18632-18637(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
[15]"Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease."
Pearson M.A., Michel L.O., Hausinger R.P., Karplus P.A.
Biochemistry 36:8164-8172(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND ACETOHYDROXAMIC ACID.
[16]"Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand."
Pearson M.A., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P.
Biochemistry 37:6214-6220(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA; UREC AND FORMATE.
[17]"Characterization of metal-substituted Klebsiella aerogenes urease."
Yamaguchi K., Cosper N.J., Staalhandske C., Scott R.A., Pearson M.A., Karplus P.A., Hausinger R.P.
J. Biol. Inorg. Chem. 4:468-477(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA AND UREC.
[18]"Kinetic and structural characterization of urease active site variants."
Pearson M.A., Park I.-S., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P.
Biochemistry 39:8575-8584(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA AND UREC, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36068 Genomic DNA. Translation: AAA25150.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5KX-ray2.20B1-101[»]
1A5LX-ray2.20B1-101[»]
1A5MX-ray2.00B1-101[»]
1A5NX-ray2.40B1-101[»]
1A5OX-ray2.50B1-101[»]
1EF2X-ray2.50B1-101[»]
1EJRX-ray2.00B1-101[»]
1EJSX-ray2.00B1-101[»]
1EJTX-ray2.00B1-101[»]
1EJUX-ray2.00B1-101[»]
1EJVX-ray2.40B1-101[»]
1EJWX-ray1.90B1-101[»]
1EJXX-ray1.60B1-101[»]
1FWAX-ray2.00B1-106[»]
1FWBX-ray2.00B1-106[»]
1FWCX-ray2.00B1-106[»]
1FWDX-ray2.00B1-106[»]
1FWEX-ray2.00B1-106[»]
1FWFX-ray2.00B1-106[»]
1FWGX-ray2.00B1-106[»]
1FWHX-ray2.00B1-106[»]
1FWIX-ray2.00B1-106[»]
1FWJX-ray2.20B1-106[»]
1KRAX-ray2.30B1-106[»]
1KRBX-ray2.50B1-106[»]
1KRCX-ray2.50B1-106[»]
2KAUX-ray2.00B1-106[»]
4EP8X-ray1.55B1-101[»]
4EPBX-ray1.75B1-101[»]
4EPDX-ray1.70B1-101[»]
4EPEX-ray2.05B1-101[»]
ProteinModelPortalP18315.
SMRP18315. Positions 1-101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP18315. 2 interactions.

Protein family/group databases

MEROPSM38.982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP18315.
UniPathwayUPA00258; UER00370.

Family and domain databases

Gene3D2.10.150.10. 1 hit.
HAMAPMF_01954. Urease_beta.
InterProIPR002019. Urease_beta.
[Graphical view]
PfamPF00699. Urease_beta. 1 hit.
[Graphical view]
SUPFAMSSF51278. SSF51278. 1 hit.
TIGRFAMsTIGR00192. urease_beta. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP18315.

Entry information

Entry nameURE2_ENTAE
AccessionPrimary (citable) accession number: P18315
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways