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UniProtKB/Swiss-Prot entry P14916


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name URE23_HELPY
Primary accession number P14916
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on May 1, 1992 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 84)
Name and origin of the protein
Protein name Urease subunit alpha
Synonyms EC 3.5.1.5
Urea amidohydrolase subunit alpha
Gene name
Name: ureA
Synonyms: hpuA
OrderedLocusNames: HP_0073
From
Helicobacter pylori (Campylobacter pylori) [TaxID: 210] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Helicobacteraceae; Helicobacter.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CPM630;
DOI=10.1093/nar/18.2.362; PubMed=2326167 [NCBI, ExPASy, EBI, Israel, Japan]
Clayton C.L., Pallen M.J., Kleanthous H., Wren B.W., Tabaqchali S.;
"Nucleotide sequence of two genes from Helicobacter pylori encoding for urease subunits.";
Nucleic Acids Res. 18:362-362(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=85P;
PubMed=2001995 [NCBI, ExPASy, EBI, Israel, Japan]
Labigne A., Cussac V., Courcoux P.;
"Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity.";
J. Bacteriol. 173:1920-1931(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=HPK5;
PubMed=10844692 [NCBI, ExPASy, EBI, Israel, Japan]
Akada J.K., Shirai M., Takeuchi H., Tsuda M., Nakazawa T.;
"Identification of the urease operon in Helicobacter pylori and its control by mRNA decay in response to pH.";
Mol. Microbiol. 36:1071-1084(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700392 / 26695;
DOI=10.1038/41483; PubMed=9252185 [NCBI, ExPASy, EBI, Israel, Japan]
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
"The complete genome sequence of the gastric pathogen Helicobacter pylori.";
Nature 388:539-547(1997).
[5]
PROTEIN SEQUENCE OF 1-20.
PubMed=2318539 [NCBI, ExPASy, EBI, Israel, Japan]
Hu L.-T., Mobley H.L.T.;
"Purification and N-terminal analysis of urease from Helicobacter pylori.";
Infect. Immun. 58:992-998(1990).
[6]
PROTEIN SEQUENCE OF 1-20, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INTERACTION WITH UREB.
PubMed=2188975 [NCBI, ExPASy, EBI, Israel, Japan]
Dunn B.E., Campbell G.P., Perez-Perez G.I., Blaser M.J.;
"Purification and characterization of urease from Helicobacter pylori.";
J. Biol. Chem. 265:9464-9469(1990).
[7]
PROTEIN SEQUENCE OF 1-20.
STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
PubMed=1452359 [NCBI, ExPASy, EBI, Israel, Japan]
Turbett G.R., Hoej P.B., Horne R., Mee B.J.;
"Purification and characterization of the urease enzymes of Helicobacter species from humans and animals.";
Infect. Immun. 60:5259-5266(1992).
[8]
KNOCKOUT.
STRAIN=85P;
PubMed=1313413 [NCBI, ExPASy, EBI, Israel, Japan]
Cussac V., Ferrero R.L., Labigne A.;
"Expression of Helicobacter pylori urease genes in Escherichia coli grown under nitrogen-limiting conditions.";
J. Bacteriol. 174:2466-2473(1992).
[9]
CATALYTIC ACTIVITY.
PubMed=1612735 [NCBI, ExPASy, EBI, Israel, Japan]
Hu L.-T., Foxall P.A., Russell R., Mobley H.L.T.;
"Purification of recombinant Helicobacter pylori urease apoenzyme encoded by ureA and ureB.";
Infect. Immun. 60:2657-2666(1992).
[10]
FUNCTION.
PubMed=8039935 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuda M., Karita M., Morshed M.G., Okita K., Nakazawa T.;
"A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach.";
Infect. Immun. 62:3586-3589(1994).
[11]
SUBCELLULAR LOCATION.
PubMed=8641799 [NCBI, ExPASy, EBI, Israel, Japan]
Phadnis S.H., Parlow M.H., Levy M., Ilver D., Caulkins C.M., Connors J.B., Dunn B.E.;
"Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis.";
Infect. Immun. 64:905-912(1996).
[12]
INDUCTION.
DOI=10.1128/IAI.69.8.4891-4897.2001; PubMed=11447165 [NCBI, ExPASy, EBI, Israel, Japan]
van Vliet A.H.M., Kuipers E.J., Waidner B., Davies B.J., de Vries N., Penn C.W., Vandenbroucke-Grauls C.M.J.E., Kist M., Bereswill S., Kusters J.G.;
"Nickel-responsive induction of urease expression in Helicobacter pylori is mediated at the transcriptional level.";
Infect. Immun. 69:4891-4897(2001).
[13]
REVIEW ON VIRULENCE OF H.PYLORI.
DOI=10.1111/j.1574-6968.2007.00648.x; PubMed=17313591 [NCBI, ExPASy, EBI, Israel, Japan]
Clyne M., Dolan B., Reeves E.P.;
"Bacterial factors that mediate colonization of the stomach and virulence of Helicobacter pylori.";
FEMS Microbiol. Lett. 268:135-143(2007).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT STRUCTURE, AND PH DEPENDENCE.
DOI=10.1038/88563; PubMed=11373617 [NCBI, ExPASy, EBI, Israel, Japan]
Ha N.-C., Oh S.-T., Sung J.Y., Cha K.A., Lee M.H., Oh B.-H.;
"Supramolecular assembly and acid resistance of Helicobacter pylori urease.";
Nat. Struct. Biol. 8:505-509(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X17079; CAA34932.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60398; AAA25020.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB032429; BAA84532.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000511; AAD07144.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38537; URKCAP.
RefSeq NP_206873.1; -.
3D structure databases
PDB
1E9Y; X-ray; 3.00 A; A=1-238.[ExPASy / RCSB / EBI]
1E9Z; X-ray; 3.00 A; A=1-238.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E9Y; -.
1E9Z; -.
ModBase P14916.
Protein-protein interaction databases
DIP DIP:3146N; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0009039; Molecular function: urease activity (inferred from electronic annotation from HAMAP).
GO:0019627; Biological process: urea metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01955; -; 1.
PBIL [Tree]
InterPro IPR002019; Urease_beta.
IPR002026; Urease_gamma_reg.
IPR008223; Urease_gammabeta.
Graphical view of domain structure.
Gene3D G3DSA:2.10.150.10; Urease_beta; 1.
G3DSA:3.30.280.10; Urease_gamma_reg; 1.
Pfam PF00699; Urease_beta; 1.
PF00547; Urease_gamma; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001225; Urease_gammabeta; 1.
ProDom PD002326; Urease_beta; 1.
PD002319; Urease_gamma; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00192; urease_beta; 1.
TIGR00193; urease_gam; 1.
BLOCKS P14916.
Genome annotation databases
GeneID 900171; -.
GenomeReviews AE000511_GR; HP_0073.
KEGG hpy:HP0073; -.
NMPDR fig|85962.1.peg.71; -.
TIGR HP_0073; -.
Phylogenomic databases
HOGENOM P14916; -.
Other
ProtoNet P14916.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Virulence.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   238  238     Urease subunit alpha. PRO_0000098075
REGION   1   102  102     Urease gamma. 
REGION   103   238  136     Urease beta. 
CONFLICT   14    14        H -> S (in Ref. 5; AA sequence). 
CONFLICT   37    37        A -> R (in Ref. 1; CAA34932). 
CONFLICT   49    49        A -> R (in Ref. 1; CAA34932). 
CONFLICT   132   133        KN -> PP (in Ref. 1; CAA34932). 
HELIX   5    25  21      
HELIX   32    49  18      
HELIX   54    60  7      
HELIX   61    63  3      
TURN   67    69  3      
HELIX   74    77  4      
STRAND   80    87  8      
STRAND   90    97  8      
STRAND   117   119  3      
TURN   120   123  4      
STRAND   128   133  6      
STRAND   135   137  3      
STRAND   139   142  4      
HELIX   147   149  3      
STRAND   154   156  3      
HELIX   158   161  4      
STRAND   164   166  3      
STRAND   173   176  4      
STRAND   181   188  8      
HELIX   208   221  14      
Sequence information
Length: 238 AA [This is the length of the unprocessed precursor] Molecular weight: 26540 Da [This is the MW of the unprocessed precursor] CRC64: 4E77328669CD9A2D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLTPKELDK LMLHYAGELA KKRKEKGIKL NYVEAVALIS AHIMEEARAG KKTAAELMQE 

        70         80         90        100        110        120 
GRTLLKPDDV MDGVASMIHE VGIEAMFPDG TKLVTVHTPI EANGKLVPGE LFLKNEDITI 

       130        140        150        160        170        180 
NEGKKAVSVK VKNVGDRPVQ IGSHFHFFEV NRCLDFDREK TFGKRLDIAS GTAVRFEPGE 

       190        200        210        220        230 
EKSVELIDIG GNRRIFGFNA LVDRQADNES KKIALHRAKE RGFHGAKSDD NYVKTIKE 

P14916 in FASTA format

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