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P18315

- URE2_ENTAE

UniProt

P18315 - URE2_ENTAE

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Protein

Urease subunit beta

Gene
ureB
Organism
Enterobacter aerogenes (Aerobacter aerogenes)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.9 Publications

Enzyme regulationi

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.4 Publications

Kineticsi

  1. KM=2.3 mM for urea4 Publications

Vmax=1.9 mmol/min/mg enzyme

pH dependencei

Optimum pH is 7.75.

Pathwayi

GO - Molecular functioni

  1. urease activity Source: UniProtKB-EC

GO - Biological processi

  1. urea catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

SABIO-RKP18315.
UniPathwayiUPA00258; UER00370.

Protein family/group databases

MEROPSiM38.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit beta (EC:3.5.1.5)
Alternative name(s):
Urea amidohydrolase subunit beta
Gene namesi
Name:ureB
OrganismiEnterobacter aerogenes (Aerobacter aerogenes)
Taxonomic identifieri548 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391H → A: Reduces activity by 20% and reduces thermal stability above 50 degrees Celsius. 1 Publication
Mutagenesisi41 – 411H → A: Reduces activity by 30% and reduces thermal stability above 50 degrees Celsius. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 106106Urease subunit betaUniRule annotationPRO_0000067577Add
BLAST

Interactioni

Subunit structurei

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.5 Publications

Protein-protein interaction databases

IntActiP18315. 2 interactions.

Structurei

Secondary structure

1
106
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 144
Beta strandi21 – 288
Beta strandi30 – 323
Beta strandi34 – 374
Helixi42 – 443
Beta strandi49 – 513
Turni53 – 586
Beta strandi59 – 613
Beta strandi68 – 714
Beta strandi76 – 838

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP18315.
SMRiP18315. Positions 1-101.

Miscellaneous databases

EvolutionaryTraceiP18315.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.10.150.10. 1 hit.
HAMAPiMF_01954. Urease_beta.
InterProiIPR002019. Urease_beta.
[Graphical view]
PfamiPF00699. Urease_beta. 1 hit.
[Graphical view]
SUPFAMiSSF51278. SSF51278. 1 hit.
TIGRFAMsiTIGR00192. urease_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

P18315-1 [UniParc]FASTAAdd to Basket

« Hide

MIPGEYHVKP GQIALNTGRA TCRVVVENHG DRPIQVGSHY HFAEVNPALK    50
FDRQQAAGYR LNIPAGTAVR FEPGQKREVE LVAFAGHRAV FGFRGEVMGP 100
LEVNDE 106
Length:106
Mass (Da):11,695
Last modified:November 1, 1990 - v1
Checksum:iA232BFCD74864EA6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M36068 Genomic DNA. Translation: AAA25150.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M36068 Genomic DNA. Translation: AAA25150.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A5K X-ray 2.20 B 1-101 [» ]
1A5L X-ray 2.20 B 1-101 [» ]
1A5M X-ray 2.00 B 1-101 [» ]
1A5N X-ray 2.40 B 1-101 [» ]
1A5O X-ray 2.50 B 1-101 [» ]
1EF2 X-ray 2.50 B 1-101 [» ]
1EJR X-ray 2.00 B 1-101 [» ]
1EJS X-ray 2.00 B 1-101 [» ]
1EJT X-ray 2.00 B 1-101 [» ]
1EJU X-ray 2.00 B 1-101 [» ]
1EJV X-ray 2.40 B 1-101 [» ]
1EJW X-ray 1.90 B 1-101 [» ]
1EJX X-ray 1.60 B 1-101 [» ]
1FWA X-ray 2.00 B 1-106 [» ]
1FWB X-ray 2.00 B 1-106 [» ]
1FWC X-ray 2.00 B 1-106 [» ]
1FWD X-ray 2.00 B 1-106 [» ]
1FWE X-ray 2.00 B 1-106 [» ]
1FWF X-ray 2.00 B 1-106 [» ]
1FWG X-ray 2.00 B 1-106 [» ]
1FWH X-ray 2.00 B 1-106 [» ]
1FWI X-ray 2.00 B 1-106 [» ]
1FWJ X-ray 2.20 B 1-106 [» ]
1KRA X-ray 2.30 B 1-106 [» ]
1KRB X-ray 2.50 B 1-106 [» ]
1KRC X-ray 2.50 B 1-106 [» ]
2KAU X-ray 2.00 B 1-106 [» ]
4EP8 X-ray 1.55 B 1-101 [» ]
4EPB X-ray 1.75 B 1-101 [» ]
4EPD X-ray 1.70 B 1-101 [» ]
4EPE X-ray 2.05 B 1-101 [» ]
ProteinModelPortali P18315.
SMRi P18315. Positions 1-101.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P18315. 2 interactions.

Protein family/group databases

MEROPSi M38.982.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00258 ; UER00370 .
SABIO-RK P18315.

Miscellaneous databases

EvolutionaryTracei P18315.

Family and domain databases

Gene3Di 2.10.150.10. 1 hit.
HAMAPi MF_01954. Urease_beta.
InterProi IPR002019. Urease_beta.
[Graphical view ]
Pfami PF00699. Urease_beta. 1 hit.
[Graphical view ]
SUPFAMi SSF51278. SSF51278. 1 hit.
TIGRFAMsi TIGR00192. urease_beta. 1 hit.
ProtoNeti Search...

Publicationsi

  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. 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. 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.

Entry informationi

Entry nameiURE2_ENTAE
AccessioniPrimary (citable) accession number: P18315
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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