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P0C7K7 (URE1_UREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 alpha

EC=3.5.1.5
Alternative name(s):
Urea amidohydrolase subunit alpha
Gene names
Name:ureC
Ordered Locus Names:UU432
OrganismUreaplasma parvum serovar 3 (strain ATCC 700970) [Complete proteome] [HAMAP]
Taxonomic identifier273119 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeUreaplasma

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953

Cofactor

Binds 2 nickel ions per subunit By similarity. HAMAP MF_01953

Pathway

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

Subunit structure

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

Subcellular location

Cytoplasm By similarity HAMAP MF_01953.

Post-translational modification

Carbamylation allows a single lysine to coordinate two nickel ions By similarity. HAMAP MF_01953

Sequence similarities

Belongs to the urease family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processurea metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnickel cation binding

Inferred from electronic annotation. Source: InterPro

urease activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598Urease subunit alpha HAMAP MF_01953
PRO_0000067563

Sites

Active site3261Proton donor By similarity
Metal binding1411Nickel 2 By similarity
Metal binding1431Nickel 2 By similarity
Metal binding2231Nickel 1; via carbamate group By similarity
Metal binding2231Nickel 2; via carbamate group By similarity
Metal binding2521Nickel 1 By similarity
Metal binding2781Nickel 1 By similarity
Metal binding3661Nickel 2 By similarity
Binding site2251Substrate By similarity

Amino acid modifications

Modified residue2231N6-carboxylysine By similarity

Experimental info

Sequence conflict1001I → L in AAA89189. Ref.1
Sequence conflict2441K → N in AAD28136. Ref.4
Sequence conflict2441K → N in AAD28139. Ref.4
Sequence conflict3551H → A in AAA89189. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0C7K7 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 5760DA36AC021424

FASTA59864,545
        10         20         30         40         50         60 
MFKISRKNYS DLYGITTGDS VRLGDTNLWV KVEKDLTTYG EESVFGGGKT LREGMGMNST 

        70         80         90        100        110        120 
MKLDDKLGNA EVMDLVITNA LIVDYTGIYK ADIGIKNGKI AAIGKSGNPH LTDNVDMIVG 

       130        140        150        160        170        180 
ISTEISAGEG KIYTAGGLDT HVHWLEPEIV PVALDGGITT VIAGGTGMND GTKATTVSPG 

       190        200        210        220        230        240 
KFWVKSALQA ADGLSINAGF LAKGQGMEDP IFEQIAAGAC GLKIHEDWGA TGNAIDLALT 

       250        260        270        280        290        300 
VADKTDVAVA IHTDTLNEAG FVEHTIAAMK GRTIHAYHTE GAGGGHAPDI LETVKYAHIL 

       310        320        330        340        350        360 
PASTNPTIPY TVNTIAEHLD MLMVCHHLNP KVPEDVAFAD SRIRSQTIAA EDLLHDMGAI 

       370        380        390        400        410        420 
SIMSSDTLAM GRIGEVATRT WQMAHKMKAQ FGSLKGDSEF SDNNRVKRYI SKYTINPAIA 

       430        440        450        460        470        480 
HGVDSYIGSL EVGKLADIVA WEPKFFGAKP YYVVKMGVIA RCVAGDPNAS IPTCEPVIMR 

       490        500        510        520        530        540 
DQFGTYGRLL TNTSVSFVSK IGLENGIKEE YKLEKELLPV KNCRSVNKKS MKWNSATPNL 

       550        560        570        580        590 
EVDPQTFDAA VDFNDLENWL EQSASELAKK LKKTSSGKYI LDAEPLTEAP LAQRYFLF 

« Hide

References

« Hide 'large scale' references
[1]"Organization of Ureaplasma urealyticum urease gene cluster and expression in a suppressor strain of Escherichia coli."
Neyrolles O., Ferris S., Behbahani N., Montagnier L., Blanchard A.
J. Bacteriol. 178:647-655(1996) [PubMed: 8550495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27813 / 7 / Serovar 1.
[2]Erratum
Neyrolles O., Ferris S., Behbahani N., Montagnier L., Blanchard A.
J. Bacteriol. 178:2725-2725(1996) [PubMed: 8626347] [Abstract]
[3]"The complete sequence of the mucosal pathogen Ureaplasma urealyticum."
Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., Cassell G.H.
Nature 407:757-762(2000) [PubMed: 11048724] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700970.
[4]"Phylogenetic study of Ureaplasma parvum and Ureaplasma urealyticum."
Kong F., Gilbert G.L.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Phylogenetic analysis of Ureaplasma urealyticum -- support for the establishment of a new species, Ureaplasma parvum."
Kong F., James G., Ma Z., Gordon S., Wang B., Gilbert G.L.
Int. J. Syst. Bacteriol. 49:1879-1889(1999) [PubMed: 10555372] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
Strain: ATCC 27813 / 7 / Serovar 1, ATCC 27818 / Pi / Serovar 6 and ATCC 33697 / U26 / Serovar 14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L40489 Genomic DNA. Translation: AAA89189.2.
AF222894 Genomic DNA. Translation: AAF30844.1.
AF085730 Genomic DNA. Translation: AAD28136.2.
AF085731 Genomic DNA. Translation: AAD28139.2.
AF085733 Genomic DNA. Translation: AAD28145.2.
PIRG82890.
RefSeqNP_078269.1. NC_002162.1.

3D structure databases

ProteinModelPortalP0C7K7.
SMRP0C7K7. Positions 1-552.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID876212.
GenomeReviewsGene locus UU432 in contig AF222894_GR.
KEGGuur:UU432.
PATRIC20534447. VBIUrePar45146_0448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG357507.
OMATIHAFHT.
ProtClustDBPRK13207.

Family and domain databases

HAMAPMF_01953. Urease_alpha.
[Tree]
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]
KOK01428.
PfamPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSPR01752. UREASE.
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01792. Urease_alph. 1 hit.
PROSITEPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameURE1_UREPA
AccessionPrimary (citable) accession number: P0C7K7
Secondary accession number(s): Q60058, Q9PQ56, Q9R3U4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 25 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

SIMILARITY comments

Index of protein domains and families