Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P17089 (URED_PROMH)

Last modified June 16, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Urease accessory protein ureD
Gene names
Name: ureD
Ordered Locus Names: PMI3682
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for maturation of urease via the functional incorporation of the urease nickel metallocenter By similarity.

Subunit structure

UreD, ureF and ureG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of ureC. The ureE protein probably delivers the nickel By similarity.

Subcellular location

Cytoplasm By similarity.

Induction

By urea. Ref.4

Sequence similarities

Belongs to the ureD family.

Ontologies

Keywords
   Biological processNickel insertion
   Cellular componentCytoplasm
   Molecular functionChaperone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processnitrogen compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnickel ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 274274Urease accessory protein ureD HAMAP MF_01384
PRO_0000067613

Experimental info

Mutagenesis2701R → RRRRI: Reduces activity 14-fold. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P17089-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 5B52FAAFD3573A9E

FASTA27431,009
        10         20         30         40         50         60 
MPDFSEKGWL ADIALRYELK RGKTCLTEKR HLGPLMVQRP FYPEQGVAHT YLLHPPGGVV 

        70         80         90        100        110        120 
GGDTLSININ VQPYAHALLT TPGATKFYRS AGGTASQTQT LTVAQEGFLE WLPQENIFFP 

       130        140        150        160        170        180 
DAQVCLTTHI HLASSAKFIG WEMQCFGRPV LNEWFETGKV KGRLNFYVDE RLILTESMRV 

       190        200        210        220        230        240 
EGLQKQAAAM REFPMFGSLY IYPATDALKE IIQHHLEKVN PLVEYGLTDV DGILVLRVLG 

       250        260        270 
TQTEPMMACF AQVWQIVRQH WLGYCPEPPR IWAT 

« Hide

References

« Hide 'large scale' references
[1]"Proteus mirabilis urease: nucleotide sequence determination and comparison with jack bean urease."
Jones B.D., Mobley H.L.T.
J. Bacteriol. 171:6414-6422(1989) [PubMed: 2687233] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed: 18375554] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Construction of a urease-negative mutant of Proteus mirabilis: analysis of virulence in a mouse model of ascending urinary tract infection."
Jones B.D., Lockatell C.V., Johnson D.E., Warren J.W., Mobley H.L.T.
Infect. Immun. 58:1120-1123(1990) [PubMed: 2180821] [Abstract]
Cited for: UREASE AS A VIRULENCE FACTOR.
[4]"Proteus mirabilis urease: transcriptional regulation by UreR."
Nicholson E.B., Concaugh E.A., Foxall P.A., Island M.D., Mobley H.L.T.
J. Bacteriol. 175:465-473(1993) [PubMed: 7678244] [Abstract]
Cited for: INDUCTION.
[5]"Proteus mirabilis urease: operon fusion and linker insertion analysis of ure gene organization, regulation, and function."
Island M.D., Mobley H.L.T.
J. Bacteriol. 177:5653-5660(1995) [PubMed: 7559355] [Abstract]
Cited for: PROBABLE OPERON STRUCTURE, MUTAGENESIS OF ARG-270.

Cross-references

Sequence databases

M31834 Genomic DNA. Translation: AAA25666.1.
AM942759 Genomic DNA. Translation: CAR47180.1.
PIRA43719.
RefSeqYP_002153357.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6801576.
GenomeReviewsGene locus PMI3682 in contig AM942759_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAP17089. PQSSIFF.

Family and domain databases

HAMAPMF_01384.
[Tree]
InterProIPR002669. UreD.
[Graphical view]
PfamPF01774. UreD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameURED_PROMH
AccessionPrimary (citable) accession number: P17089
Secondary accession number(s): B4EXN2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents