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UniProtKB/Swiss-Prot entry P69996


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

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Entry information
Entry name URE1_HELPY
Primary accession number P69996
Secondary accession numbers P14917 Q9R3B3
Integrated into Swiss-Prot on January 4, 2005
Sequence was last modified on January 4, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 39)
Name and origin of the protein
Protein name Urease subunit beta
Synonyms EC 3.5.1.5
Urea amidohydrolase subunit beta
Gene name
Name: ureB
Synonyms: hpuB
OrderedLocusNames: HP_0072
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=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).
[2]
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).
[3]
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).
[4]
PROTEIN SEQUENCE OF 1-30, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS.
DOI=10.1016/0882-4010(91)90062-F; PubMed=1857197 [NCBI, ExPASy, EBI, Israel, Japan]
Evans D.J. Jr., Evans D.G., Kirkpatrick S.S., Graham D.Y.;
"Characterization of the Helicobacter pylori urease and purification of its subunits.";
Microb. Pathog. 10:15-26(1991).
[5]
PROTEIN SEQUENCE OF 1-20, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND INTERACTION WITH UREA.
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).
[6]
PROTEIN SEQUENCE OF 1-15.
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).
[7]
PROTEIN SEQUENCE OF 1-12.
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 565-569, AND 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, AND ROLE IN VIRULENCE.
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]
INDUCTION.
DOI=10.1099/mic.0.28188-0; PubMed=16339943 [NCBI, ExPASy, EBI, Israel, Japan]
Belzer C., Stoof J., Beckwith C.S., Kuipers E.J., Kusters J.G., van Vliet A.H.M.;
"Differential regulation of urease activity in Helicobacter hepaticus and Helicobacter pylori.";
Microbiology 151:3989-3995(2005).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH NICKEL IONS, SUBUNIT STRUCTURE, AND CARBAMYLATION AT LYS-219.
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
M60398; AAA25021.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X17079; CAA34933.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000511; AAD07143.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M84338; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR B38537; URKCBP.
RefSeq NP_206872.1; -.
3D structure databases
PDB
1E9Y; X-ray; 3.00 A; B=1-569.[ExPASy / RCSB / EBI]
1E9Z; X-ray; 3.00 A; B=1-569.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E9Y; -.
1E9Z; -.
ModBase P69996.
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_01953; -; 1.
PBIL [Tree]
InterPro IPR006680; Amidohydro_1.
IPR005848; Urease_alpha.
IPR011612; Urease_alpha_N.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
PF00449; Urease_alpha; 1.
Pfam graphical view of domain structure.
PRINTS PR01752; UREASE.
TIGRFAMs TIGR01792; urease_alph; 1.
PROSITE PS01120; UREASE_1; 1.
PS00145; UREASE_2; 1.
PS51368; UREASE_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P69996.
Genome annotation databases
GeneID 899104; -.
GenomeReviews AE000511_GR; HP_0072.
KEGG hpy:HP0072; -.
TIGR HP_0072; -.
Phylogenomic databases
HOGENOM P69996; -.
Other
ProtoNet P69996.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Nickel; Virulence.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   569  569     Urease subunit beta. PRO_0000067533
DOMAIN   131   569  439     Urease. 
ACT_SITE   322   322        Proton donor (Probable). 
METAL   136   136        Nickel 2. 
METAL   138   138        Nickel 2. 
METAL   219   219        Nickel 1; via carbamate group. 
METAL   219   219        Nickel 2; via carbamate group. 
METAL   248   248        Nickel 1. 
METAL   274   274        Nickel 1. 
METAL   362   362        Nickel 2. 
BINDING   221   221        Substrate (Probable). 
MOD_RES   219   219        N6-carboxylysine. 
CONFLICT   10    10        V -> A (in Ref. 2; CAA34933). 
CONFLICT   19    19        D -> A (in Ref. 2). 
CONFLICT   22    22        R -> C (in Ref. 4; AA sequence). 
CONFLICT   27    27        D -> C (in Ref. 4; AA sequence). 
CONFLICT   104   104        M -> T (in Ref. 2; CAA34933). 
CONFLICT   181   181        W -> F (in Ref. 2; CAA34933). 
CONFLICT   193   193        L -> F (in Ref. 2; CAA34933). 
CONFLICT   218   218        F -> L (in Ref. 2; CAA34933). 
CONFLICT   273   273        F -> Y (in Ref. 2; CAA34933). 
CONFLICT   540   540        P -> S (in Ref. 2; CAA34933). 
CONFLICT   554   569        SKPANKVSLAQLFSIF -> LNQPIK (in Ref. 2; CAA34933). 
STRAND   3     5  3      
HELIX   6    10  5      
STRAND   20    22  3      
STRAND   29    31  3      
TURN   54    56  3      
STRAND   67    77  11      
STRAND   80    89  10      
STRAND   92    97  6      
TURN   102   104  3      
STRAND   105   107  3      
HELIX   110   112  3      
STRAND   119   122  4      
STRAND   127   130  4      
STRAND   132   138  7      
HELIX   144   150  7      
STRAND   153   159  7      
HELIX   165   169  5      
HELIX   175   186  12      
STRAND   189   198  10      
HELIX   204   212  9      
STRAND   216   220  5      
HELIX   222   224  3      
HELIX   228   240  13      
STRAND   244   247  4      
HELIX   258   265  8      
STRAND   270   272  3      
TURN   273   276  4      
TURN   283   285  3      
HELIX   286   291  6      
STRAND   295   299  5      
HELIX   301   303  3      
HELIX   310   320  11      
TURN   321   323  3      
HELIX   329   338  10      
HELIX   341   352  12      
HELIX   372   387  16      
STRAND   395   397  3      
HELIX   399   406  8      
HELIX   407   409  3      
HELIX   411   416  6      
TURN   420   422  3      
STRAND   423   426  4      
STRAND   434   437  4      
TURN   439   444  6      
STRAND   447   451  5      
STRAND   454   460  7      
STRAND   465   468  4      
STRAND   474   477  4      
HELIX   479   481  3      
HELIX   485   489  5      
STRAND   491   494  4      
HELIX   496   500  5      
HELIX   503   506  4      
STRAND   511   515  5      
HELIX   524   526  3      
STRAND   536   538  3      
TURN   540   542  3      
STRAND   545   547  3      
STRAND   561   563  3      
TURN   564   566  3      
Sequence information
Length: 569 AA [This is the length of the unprocessed precursor] Molecular weight: 61684 Da [This is the MW of the unprocessed precursor] CRC64: 4C8A6BC6C8295584 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKISRKEYV SMYGPTTGDK VRLGDTDLIA EVEHDYTIYG EELKFGGGKT LREGMSQSNN 

        70         80         90        100        110        120 
PSKEELDLII TNALIVDYTG IYKADIGIKD GKIAGIGKGG NKDMQDGVKN NLSVGPATEA 

       130        140        150        160        170        180 
LAGEGLIVTA GGIDTHIHFI SPQQIPTAFA SGVTTMIGGG TGPADGTNAT TITPGRRNLK 

       190        200        210        220        230        240 
WMLRAAEEYS MNLGFLAKGN ASNDASLADQ IEAGAIGFKI HEDWGTTPSA INHALDVADK 

       250        260        270        280        290        300 
YDVQVAIHTD TLNEAGCVED TMAAIAGRTM HTFHTEGAGG GHAPDIIKVA GEHNILPAST 

       310        320        330        340        350        360 
NPTIPFTVNT EAEHMDMLMV CHHLDKSIKE DVQFADSRIR PQTIAAEDTL HDMGIFSITS 

       370        380        390        400        410        420 
SDSQAMGRVG EVITRTWQTA DKNKKEFGRL KEEKGDNDNF RIKRYLSKYT INPAIAHGIS 

       430        440        450        460        470        480 
EYVGSVEVGK VADLVLWSPA FFGVKPNMII KGGFIALSQM GDANASIPTP QPVYYREMFA 

       490        500        510        520        530        540 
HHGKAKYDAN ITFVSQAAYD KGIKEELGLE RQVLPVKNCR NITKKDMQFN DTTAHIEVNP 

       550        560 
ETYHVFVDGK EVTSKPANKV SLAQLFSIF 

P69996 in FASTA format

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