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P41021 (URE2_SPOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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
OrganismSporosarcina pasteurii (Bacillus pasteurii)
Taxonomic identifier1474 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPlanococcaceaeSporosarcina

Protein attributes

Sequence length126 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP-Rule MF_01954

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.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01954.

Sequence similarities

Belongs to the urease beta subunit family.

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 – 126126Urease subunit beta HAMAP-Rule MF_01954
PRO_0000067569

Secondary structure

.......................... 126
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41021 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E1BE8E5209586B02

FASTA12613,959
        10         20         30         40         50         60 
MSNNNYIVPG EYRVAEGEIE INAGREKTTI RVSNTGDRPI QVGSHIHFVE VNKELLFDRA 

        70         80         90        100        110        120 
EGIGRRLNIP SGTAARFEPG EEMEVELTEL GGNREVFGIS DLTNGSVDNK ELILQRAKEL 


GYKGVE 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78411 Genomic DNA. Translation: CAA55174.1.
PIRS47103.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP41021.
SMRP41021. Positions 5-126.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP41021.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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

EvolutionaryTraceP41021.

Entry information

Entry nameURE2_SPOPA
AccessionPrimary (citable) accession number: P41021
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 19, 2014
This is version 83 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