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Protein

Urease subunit beta

Gene

ureB

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

Functioni

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.UniRule annotation

Pathway: urea degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and NH(3) from urea (urease route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Urease subunit gamma (ureA), Urease subunit beta (ureB), Urease subunit alpha (ureC), Urease (ureC)
This subpathway is part of the pathway urea degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from urea (urease route), the pathway urea degradation and in Nitrogen metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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

Complete GO annotation...

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.UniRule annotation5 Publications

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4CEUX-ray1.58B1-126[»]
4CEXX-ray1.59B1-126[»]
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

        10         20         30         40         50
MSNNNYIVPG EYRVAEGEIE INAGREKTTI RVSNTGDRPI QVGSHIHFVE
60 70 80 90 100
VNKELLFDRA EGIGRRLNIP SGTAARFEPG EEMEVELTEL GGNREVFGIS
110 120
DLTNGSVDNK ELILQRAKEL GYKGVE
Length:126
Mass (Da):13,959
Last modified:February 1, 1995 - v1
Checksum:iE1BE8E5209586B02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78411 Genomic DNA. Translation: CAA55174.1.
PIRiS47103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78411 Genomic DNA. Translation: CAA55174.1.
PIRiS47103.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4CEUX-ray1.58B1-126[»]
4CEXX-ray1.59B1-126[»]
4UBPX-ray1.55B1-126[»]
ProteinModelPortaliP41021.
SMRiP41021. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP41021.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.

Miscellaneous databases

EvolutionaryTraceiP41021.

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.
ProtoNetiSearch...

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: February 4, 2015
This is version 88 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.