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P41020 (URE1_BACPA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 alpha
EC=3.5.1.5
Alternative name(s):
Urea amidohydrolase subunit alpha
Gene names
Name:ureC
OrganismBacillus pasteurii
Taxonomic identifier1474 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Planococcaceae › Sporosarcina

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP-Rule MF_01953

Cofactor

Binds 2 nickel ions per subunit.

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP-Rule MF_01953

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.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions. HAMAP-Rule MF_01953

Sequence similarities

Belongs to the urease family.

Contains 1 urease domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   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_functionnickel cation binding

Inferred from electronic annotation. Source: HAMAP

urease activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 569569Urease subunit alpha HAMAP-Rule MF_01953
PRO_0000067536

Regions

Domain131 – 569439Urease

Sites

Active site3221Proton donor Probable
Metal binding1361Nickel 2
Metal binding1381Nickel 2
Metal binding2191Nickel 1; via carbamate group
Metal binding2191Nickel 2; via carbamate group
Metal binding2481Nickel 1
Metal binding2741Nickel 1
Metal binding3621Nickel 2
Binding site2211Substrate Probable

Amino acid modifications

Modified residue2191N6-carboxylysine HAMAP-Rule MF_01953

Experimental info

Sequence conflict497 – 5015SSIQQ → ELNSE Ref.2

Secondary structure

1 ................................................................................................................ 569
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41020 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: EC55A5C4293F2E5C

FASTA56961,398
        10         20         30         40         50         60 
MKINRQQYAE SYGPTVGDRV RLADTDLGEV EKDYYYLGDE VNFGGGKVLR EGMGENGTYT 

        70         80         90        100        110        120 
RTENVLDLLL TNALILDYTG IYKADIGVKD GYIVGIGKGG NPDIMDGVTP NMIVGTATEV 

       130        140        150        160        170        180 
IAAEGKIVTA GGIDTHVHFI NPDQVDVALA NGITTLFGGG TGPAEGSKAT TVTPGPWNIE 

       190        200        210        220        230        240 
KMLKSTEGLP INVGILGKGH GSSIAPIMEQ IDAGAAGLKI HEDWGATPAS IDRSLTVADE 

       250        260        270        280        290        300 
ADVQVAIHSD TLNEAGFLED TVRAINGRVI HSFHVEGAGG GHAPDIMAMA GHPNVLPSST 

       310        320        330        340        350        360 
NPTRPFTVNT IDEHLDMLMV CHHLKQNIPE DVAFADSRIR PETIAAEDIL HDLGIISMMS 

       370        380        390        400        410        420 
TDALAMGRAG EMVLRTWQTA DKMKKQRGPL AEEKNGSDNF RLKRYVSKYT INPAIAQGMA 

       430        440        450        460        470        480 
HEVGSIEEGK FADLVLWEPK FFGVKADRVI KGGIIAYAQI GDPSASIPTP QPVMGRRMYG 

       490        500        510        520        530        540 
TVGDLIHDTN ITFMSKSSIQ QGVPAKLGLK RRIGTVKNCR NIGKKDMKWN DVTTDIDINP 

       550        560 
ETYEVKVDGE VLTCEPVKEL PMAQRYFLF

« 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]"Genetic organization and nucleotide sequence of the ure gene cluster in Bacillus pasteurii."
You J.-H., Kim J.-G., Song B.-H., Lee M.-H., Kim S.-D.
Mol. Cells 5:359-369(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 497-569.
Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
[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; UREB; NICKEL IONS AND BETA-MERCAPTOETHANOL, CARBAMYLATION AT LYS-219.
[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; UREB; NICKEL IONS AND DIAMIDOPHOSPHATE, CARBAMYLATION AT LYS-219.
[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; UREB; NICKEL IONS AND ACETOHYDROXAMIC ACID, CARBAMYLATION AT LYS-219.
[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; UREB; NICKEL AND PHOSPHATE IONS, CARBAMYLATION AT LYS-219.
[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; UREB; NICKEL AND BORATE IONS, CARBAMYLATION AT LYS-219.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X78411 Genomic DNA. Translation: CAA55175.1.
U29368 Genomic DNA. Translation: AAA73986.1.
PIRS47104.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IE7X-ray1.85C1-569[»]
1S3TX-ray2.10C1-569[»]
1UBPX-ray1.65C1-569[»]
2UBPX-ray2.00C1-569[»]
3UBPX-ray2.00C1-569[»]
4AC7X-ray1.50C1-569[»]
4UBPX-ray1.55C1-569[»]
ProteinModelPortalP41020.
SMRP41020. Positions 1-569.
ModBaseSearch...

Protein family/group databases

MEROPSM38.982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00258; UER00370.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
InterProIPR006680. Amidohydro_1.
IPR011059. Metal-dep_hydrolase_composite.
IPR011612. Urease_alpha_N.
IPR005848. Urease_asu.
IPR017951. Urease_asu_c.
IPR017950. Urease_asu_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
SUPFAMSSF51338. Metalo_hydrolase. 2 hits.
TIGRFAMsTIGR01792. urease_alph. 1 hit.
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP41020.
EvolutionaryTraceP41020.

Entry information

Entry nameURE1_BACPA
AccessionPrimary (citable) accession number: P41020
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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