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Database: UniProt
Entry: URE23_HELPY
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ID   URE23_HELPY             Reviewed;         238 AA.
AC   P14916;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 2.
DT   03-JUL-2019, entry version 152.
DE   RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01955};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01955};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01955};
GN   Name=ureA {ECO:0000255|HAMAP-Rule:MF_01955}; Synonyms=hpuA;
GN   OrderedLocusNames=HP_0073;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter
OS   pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CPM630;
RX   PubMed=2326167; DOI=10.1093/nar/18.2.362;
RA   Clayton C.L., Pallen M.J., Kleanthous H., Wren B.W., Tabaqchali S.;
RT   "Nucleotide sequence of two genes from Helicobacter pylori encoding
RT   for urease subunits.";
RL   Nucleic Acids Res. 18:362-362(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=85P;
RX   PubMed=2001995; DOI=10.1128/jb.173.6.1920-1931.1991;
RA   Labigne A., Cussac V., Courcoux P.;
RT   "Shuttle cloning and nucleotide sequences of Helicobacter pylori genes
RT   responsible for urease activity.";
RL   J. Bacteriol. 173:1920-1931(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HPK5;
RX   PubMed=10844692; DOI=10.1046/j.1365-2958.2000.01918.x;
RA   Akada J.K., Shirai M., Takeuchi H., Tsuda M., Nakazawa T.;
RT   "Identification of the urease operon in Helicobacter pylori and its
RT   control by mRNA decay in response to pH.";
RL   Mol. Microbiol. 36:1071-1084(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-20.
RX   PubMed=2318539;
RA   Hu L.-T., Mobley H.L.T.;
RT   "Purification and N-terminal analysis of urease from Helicobacter
RT   pylori.";
RL   Infect. Immun. 58:992-998(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-20, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND INTERACTION WITH UREB.
RX   PubMed=2188975;
RA   Dunn B.E., Campbell G.P., Perez-Perez G.I., Blaser M.J.;
RT   "Purification and characterization of urease from Helicobacter
RT   pylori.";
RL   J. Biol. Chem. 265:9464-9469(1990).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX   PubMed=1452359;
RA   Turbett G.R., Hoej P.B., Horne R., Mee B.J.;
RT   "Purification and characterization of the urease enzymes of
RT   Helicobacter species from humans and animals.";
RL   Infect. Immun. 60:5259-5266(1992).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=85P;
RX   PubMed=1313413; DOI=10.1128/jb.174.8.2466-2473.1992;
RA   Cussac V., Ferrero R.L., Labigne A.;
RT   "Expression of Helicobacter pylori urease genes in Escherichia coli
RT   grown under nitrogen-limiting conditions.";
RL   J. Bacteriol. 174:2466-2473(1992).
RN   [9]
RP   CATALYTIC ACTIVITY.
RX   PubMed=1612735;
RA   Hu L.-T., Foxall P.A., Russell R., Mobley H.L.T.;
RT   "Purification of recombinant Helicobacter pylori urease apoenzyme
RT   encoded by ureA and ureB.";
RL   Infect. Immun. 60:2657-2666(1992).
RN   [10]
RP   FUNCTION.
RX   PubMed=8039935;
RA   Tsuda M., Karita M., Morshed M.G., Okita K., Nakazawa T.;
RT   "A urease-negative mutant of Helicobacter pylori constructed by
RT   allelic exchange mutagenesis lacks the ability to colonize the nude
RT   mouse stomach.";
RL   Infect. Immun. 62:3586-3589(1994).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8641799;
RA   Phadnis S.H., Parlow M.H., Levy M., Ilver D., Caulkins C.M.,
RA   Connors J.B., Dunn B.E.;
RT   "Surface localization of Helicobacter pylori urease and a heat shock
RT   protein homolog requires bacterial autolysis.";
RL   Infect. Immun. 64:905-912(1996).
RN   [12]
RP   INDUCTION.
RX   PubMed=11447165; DOI=10.1128/IAI.69.8.4891-4897.2001;
RA   van Vliet A.H.M., Kuipers E.J., Waidner B., Davies B.J., de Vries N.,
RA   Penn C.W., Vandenbroucke-Grauls C.M.J.E., Kist M., Bereswill S.,
RA   Kusters J.G.;
RT   "Nickel-responsive induction of urease expression in Helicobacter
RT   pylori is mediated at the transcriptional level.";
RL   Infect. Immun. 69:4891-4897(2001).
RN   [13]
RP   REVIEW ON VIRULENCE OF H.PYLORI.
RX   PubMed=17313591; DOI=10.1111/j.1574-6968.2007.00648.x;
RA   Clyne M., Dolan B., Reeves E.P.;
RT   "Bacterial factors that mediate colonization of the stomach and
RT   virulence of Helicobacter pylori.";
RL   FEMS Microbiol. Lett. 268:135-143(2007).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT STRUCTURE, AND PH
RP   DEPENDENCE.
RX   PubMed=11373617; DOI=10.1038/88563;
RA   Ha N.-C., Oh S.-T., Sung J.Y., Cha K.A., Lee M.H., Oh B.-H.;
RT   "Supramolecular assembly and acid resistance of Helicobacter pylori
RT   urease.";
RL   Nat. Struct. Biol. 8:505-509(2001).
CC   -!- FUNCTION: Ammonia produced by ureolysis increases the gastric pH
CC       thereby providing an environment permissive for colonization of
CC       the stomach. {ECO:0000269|PubMed:8039935}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01955,
CC         ECO:0000269|PubMed:1612735, ECO:0000269|PubMed:2188975};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.48 mM for urea {ECO:0000269|PubMed:2188975};
CC         Vmax=1.1 mmol/min/mg enzyme {ECO:0000269|PubMed:2188975};
CC       pH dependence:
CC         Optimum pH is 8.0. Active from pH 4.0 to 10.0. In unbuffered
CC         solutions, the dodecameric complex is active at pH 3.0.
CC         {ECO:0000269|PubMed:11373617, ECO:0000269|PubMed:2188975};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01955}.
CC   -!- SUBUNIT: Heterohexamer of 3 UreA (alpha) and 3 UreB (beta)
CC       subunits. Four heterohexamers assemble to form a 16 nm dodecameric
CC       complex. {ECO:0000255|HAMAP-Rule:MF_01955,
CC       ECO:0000269|PubMed:11373617}.
CC   -!- INTERACTION:
CC       P69996:ureB; NbExp=2; IntAct=EBI-7737170, EBI-7566591;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01955,
CC       ECO:0000269|PubMed:8641799}. Note=Also associates with the outer
CC       membrane upon autolysis of neighboring bacteria.
CC   -!- INDUCTION: By nickel ions. {ECO:0000269|PubMed:11447165}.
CC   -!- DISRUPTION PHENOTYPE: Cells do not express urease.
CC       {ECO:0000269|PubMed:1313413}.
CC   -!- MISCELLANEOUS: The novel dodecameric structure of the enzyme may
CC       allow it to remain active at the cell surface at acidic gastric
CC       pH. Within this dodecameric structure the 12 active sites are
CC       clustered within the interior of the proteinaceous shell. This may
CC       allow a high local concentration of ammonia within the enzyme
CC       which may protect the nickel-chelating groups from protonation.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the urease gamma
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01955}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the urease beta
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01955}.
CC   -!- CAUTION: The orthologous protein is known as the gamma/beta
CC       subunit (UreAB) in most other bacteria. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Going unnoticed - Issue
CC       95 of June 2008;
CC       URL="https://web.expasy.org/spotlight/back_issues/095";
DR   EMBL; X17079; CAA34932.1; -; Genomic_DNA.
DR   EMBL; M60398; AAA25020.1; -; Genomic_DNA.
DR   EMBL; AB032429; BAA84532.1; -; Genomic_DNA.
DR   EMBL; AE000511; AAD07144.1; -; Genomic_DNA.
DR   PIR; A38537; URKCAP.
DR   RefSeq; NP_206873.1; NC_000915.1.
DR   RefSeq; WP_000779223.1; NC_018939.1.
DR   PDB; 1E9Y; X-ray; 3.00 A; A=1-238.
DR   PDB; 1E9Z; X-ray; 3.00 A; A=1-238.
DR   PDBsum; 1E9Y; -.
DR   PDBsum; 1E9Z; -.
DR   SMR; P14916; -.
DR   DIP; DIP-3146N; -.
DR   IntAct; P14916; 7.
DR   MINT; P14916; -.
DR   STRING; 85962.C694_00355; -.
DR   BindingDB; P14916; -.
DR   ChEMBL; CHEMBL3885651; -.
DR   PaxDb; P14916; -.
DR   DNASU; 900171; -.
DR   EnsemblBacteria; AAD07144; AAD07144; HP_0073.
DR   GeneID; 900171; -.
DR   KEGG; heo:C694_00355; -.
DR   KEGG; hpy:HP0073; -.
DR   PATRIC; fig|85962.47.peg.77; -.
DR   eggNOG; ENOG4108YZ9; Bacteria.
DR   eggNOG; COG0831; LUCA.
DR   eggNOG; COG0832; LUCA.
DR   KO; K14048; -.
DR   OMA; SVTSHFH; -.
DR   BioCyc; HPY:HP0073-MONOMER; -.
DR   SABIO-RK; P14916; -.
DR   UniPathway; UPA00258; UER00370.
DR   EvolutionaryTrace; P14916; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0043419; P:urea catabolic process; IMP:CACAO.
DR   CDD; cd00407; Urease_beta; 1.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   Gene3D; 3.30.280.10; -; 1.
DR   HAMAP; MF_01954; Urease_beta; 1.
DR   HAMAP; MF_01955; Urease_beta_gamma; 1.
DR   InterPro; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   InterPro; IPR008223; Urease_gamma-beta_su.
DR   InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR   InterPro; IPR036463; Urease_gamma_sf.
DR   Pfam; PF00699; Urease_beta; 1.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PIRSF; PIRSF001225; Urease_gammabeta; 1.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
DR   TIGRFAMs; TIGR00193; urease_gam; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Hydrolase; Reference proteome; Virulence.
FT   CHAIN         1    238       Urease subunit alpha.
FT                                /FTId=PRO_0000098075.
FT   REGION        1    102       Urease gamma.
FT   REGION      103    238       Urease beta.
FT   CONFLICT     14     14       H -> S (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     37     37       A -> R (in Ref. 1; CAA34932).
FT                                {ECO:0000305}.
FT   CONFLICT     49     49       A -> R (in Ref. 1; CAA34932).
FT                                {ECO:0000305}.
FT   CONFLICT    132    133       KN -> PP (in Ref. 1; CAA34932).
FT                                {ECO:0000305}.
FT   HELIX         5     25       {ECO:0000244|PDB:1E9Y}.
FT   HELIX        32     49       {ECO:0000244|PDB:1E9Y}.
FT   HELIX        54     60       {ECO:0000244|PDB:1E9Y}.
FT   HELIX        61     63       {ECO:0000244|PDB:1E9Y}.
FT   TURN         67     69       {ECO:0000244|PDB:1E9Y}.
FT   HELIX        74     77       {ECO:0000244|PDB:1E9Y}.
FT   STRAND       80     87       {ECO:0000244|PDB:1E9Y}.
FT   STRAND       90     97       {ECO:0000244|PDB:1E9Y}.
FT   STRAND      117    119       {ECO:0000244|PDB:1E9Y}.
FT   TURN        120    123       {ECO:0000244|PDB:1E9Y}.
FT   STRAND      128    133       {ECO:0000244|PDB:1E9Y}.
FT   STRAND      135    137       {ECO:0000244|PDB:1E9Y}.
FT   STRAND      139    142       {ECO:0000244|PDB:1E9Y}.
FT   HELIX       147    149       {ECO:0000244|PDB:1E9Y}.
FT   STRAND      154    156       {ECO:0000244|PDB:1E9Y}.
FT   HELIX       158    161       {ECO:0000244|PDB:1E9Y}.
FT   STRAND      164    166       {ECO:0000244|PDB:1E9Y}.
FT   STRAND      173    176       {ECO:0000244|PDB:1E9Y}.
FT   STRAND      181    188       {ECO:0000244|PDB:1E9Y}.
FT   HELIX       208    221       {ECO:0000244|PDB:1E9Y}.
SQ   SEQUENCE   238 AA;  26540 MW;  4E77328669CD9A2D CRC64;
     MKLTPKELDK LMLHYAGELA KKRKEKGIKL NYVEAVALIS AHIMEEARAG KKTAAELMQE
     GRTLLKPDDV MDGVASMIHE VGIEAMFPDG TKLVTVHTPI EANGKLVPGE LFLKNEDITI
     NEGKKAVSVK VKNVGDRPVQ IGSHFHFFEV NRCLDFDREK TFGKRLDIAS GTAVRFEPGE
     EKSVELIDIG GNRRIFGFNA LVDRQADNES KKIALHRAKE RGFHGAKSDD NYVKTIKE
//
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