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P18315

- URE2_ENTAE

UniProt

P18315 - URE2_ENTAE

Protein

Urease subunit beta

Gene

ureB

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

    Catalytic activityi

    Urea + H2O = CO2 + 2 NH3.9 PublicationsUniRule annotation

    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 enzyme4 Publications

    pH dependencei

    Optimum pH is 7.75.4 Publications

    Pathwayi

    GO - Molecular functioni

    1. urease activity Source: UniProtKB-EC

    GO - Biological processi

    1. urea catabolic process Source: UniProtKB-UniPathway

    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 betaUniRule annotation (EC:3.5.1.5UniRule annotation)
    Alternative name(s):
    Urea amidohydrolase subunit betaUniRule annotation
    Gene namesi
    Name:ureBUniRule annotation
    OrganismiEnterobacter aerogenes (Aerobacter aerogenes)
    Taxonomic identifieri548 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacter

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 betaPRO_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.12 PublicationsUniRule annotation

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18315.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the urease beta subunit family.UniRule annotation

    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: October 1, 2014
    This is version 102 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