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P41021

- URE2_SPOPA

UniProt

P41021 - URE2_SPOPA

Protein

Urease subunit beta

Gene

ureB

Organism
Sporosarcina pasteurii (Bacillus pasteurii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalytic activityi

    Urea + H2O = CO2 + 2 NH3.UniRule annotation

    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

    UniPathwayiUPA00258; UER00370.

    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
    OrganismiSporosarcina pasteurii (Bacillus pasteurii)
    Taxonomic identifieri1474 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaeSporosarcina

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 126126Urease subunit betaPRO_0000067569Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.5 PublicationsUniRule annotation

    Structurei

    Secondary structure

    1
    126
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 205
    Turni21 – 244
    Beta strandi27 – 348
    Beta strandi36 – 383
    Beta strandi40 – 434
    Helixi48 – 503
    Beta strandi55 – 573
    Helixi59 – 624
    Beta strandi65 – 673
    Beta strandi74 – 774
    Beta strandi82 – 898
    Beta strandi104 – 1063
    Helixi110 – 12011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IE7X-ray1.85B1-126[»]
    1S3TX-ray2.10B1-126[»]
    1UBPX-ray1.65B5-126[»]
    2UBPX-ray2.00B5-126[»]
    3UBPX-ray2.00B1-126[»]
    4AC7X-ray1.50B1-126[»]
    4UBPX-ray1.55B1-126[»]
    ProteinModelPortaliP41021.
    SMRiP41021. Positions 5-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41021.

    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.

    P41021-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNNNYIVPG EYRVAEGEIE INAGREKTTI RVSNTGDRPI QVGSHIHFVE    50
    VNKELLFDRA EGIGRRLNIP SGTAARFEPG EEMEVELTEL GGNREVFGIS 100
    DLTNGSVDNK ELILQRAKEL GYKGVE 126
    Length:126
    Mass (Da):13,959
    Last modified:February 1, 1995 - v1
    Checksum:iE1BE8E5209586B02
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78411 Genomic DNA. Translation: CAA55174.1.
    PIRiS47103.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78411 Genomic DNA. Translation: CAA55174.1 .
    PIRi S47103.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IE7 X-ray 1.85 B 1-126 [» ]
    1S3T X-ray 2.10 B 1-126 [» ]
    1UBP X-ray 1.65 B 5-126 [» ]
    2UBP X-ray 2.00 B 5-126 [» ]
    3UBP X-ray 2.00 B 1-126 [» ]
    4AC7 X-ray 1.50 B 1-126 [» ]
    4UBP X-ray 1.55 B 1-126 [» ]
    ProteinModelPortali P41021.
    SMRi P41021. Positions 5-126.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P41021.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00258 ; UER00370 .

    Miscellaneous databases

    EvolutionaryTracei P41021.

    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. "Nucleotide sequence of three genes on a urease encoding DNA-fragment from Bacillus pasteurii."
      Moersdorf G., Weinmann P., Kaltwasser H.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
    2. "X-ray absorption spectroscopy study of native and phenylphosphorodiamidate-inhibited Bacillus pasteurii urease."
      Benini S., Ciurli S., Nolting H.F., Mangani S.
      Eur. J. Biochem. 239:61-66(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 5-126.
    3. "Crystallization and preliminary high-resolution X-ray diffraction analysis of native and beta-mercaptoethanol-inhibited urease from Bacillus pasteurii."
      Benini S., Ciurli S., Rypniewski W.R., Wilson K.S., Mangani S.
      Acta Crystallogr. D 54:409-412(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND BETA-MERCAPTOETHANOL.
    4. "A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels."
      Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.
      Structure 7:205-216(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND DIAMIDOPHOSPHATE.
    5. "The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution."
      Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.
      J. Biol. Inorg. Chem. 5:110-118(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND ACETOHYDROXAMIC ACID.
    6. "Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism."
      Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S.
      J. Biol. Inorg. Chem. 6:778-790(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND PHOSPHATE.
    7. "Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism."
      Benini S., Rypniewski W.R., Wilson K.S., Mangani S., Ciurli S.
      J. Am. Chem. Soc. 126:3714-3715(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND BORATE IONS.

    Entry informationi

    Entry nameiURE2_SPOPA
    AccessioniPrimary (citable) accession number: P41021
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 84 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