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Protein

Urease subunit beta

Gene

ureB

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach.1 Publication

Miscellaneous

The novel dodecameric structure of the enzyme may allow it to remain active at the cell surface at acidic gastric pH. Within this dodecameric structure the 12 active sites are clustered within the interior of the proteinaceous shell. This may allow a high local concentration of ammonia within the enzyme which may protect the nickel-chelating groups from protonation.

Caution

The orthologous protein is known as the alpha subunit (UreC) in most other bacteria.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ni cationNote: Binds 2 nickel ions per subunit.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.48 mM for urea2 Publications
  1. Vmax=1.1 mmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 8.0. Active from pH 4.0 to 10.0. In unbuffered solutions, the dodecameric complex is active at pH3.0.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: urea degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and NH(3) from urea (urease route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Urease (ureA), Urease (ureB), Urease subunit alpha (ureA), Urease subunit beta (ureB)
This subpathway is part of the pathway urea degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from urea (urease route), the pathway urea degradation and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi136Nickel 1; via tele nitrogen1
Metal bindingi138Nickel 1; via tele nitrogen1
Metal bindingi219Nickel 1; via carbamate group1
Metal bindingi219Nickel 2; via carbamate group1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei221SubstrateCurated1
Metal bindingi248Nickel 2; via pros nitrogen1
Metal bindingi274Nickel 2; via tele nitrogen1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei322Proton donorCurated1
Metal bindingi362Nickel 11

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processVirulence
LigandMetal-binding, Nickel

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
HPY:HP0072-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P69996

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00258;UER00370

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M38.982

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Urease subunit betaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit betaUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ureBUniRule annotation
Synonyms:hpuB
Ordered Locus Names:HP_0072
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri85962 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000429 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells do not express urease.1 Publication

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3885651

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000675331 – 569Urease subunit betaAdd BLAST569

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei219N6-carboxylysineUniRule annotation1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Carbamylation allows a single lysine to coordinate two nickel ions.UniRule annotation1 Publication

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P69996

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By nickel ions.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterohexamer of 3 UreA (alpha) and 3 UreB (beta) subunits. Four heterohexamers assemble to form a 16 nm dodecameric complex.UniRule annotation1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ureAP149162EBI-7566591,EBI-7737170

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P69996, 13 interactors

Molecular INTeraction database

More...
MINTi
P69996

STRING: functional protein association networks

More...
STRINGi
85962.HP0072

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1569
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P69996

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P69996

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P69996

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini131 – 569UreaseUniRule annotationAdd BLAST439

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CQM Bacteria
COG0804 LUCA

KEGG Orthology (KO)

More...
KOi
K01428

Identification of Orthologs from Complete Genome Data

More...
OMAi
GFDSHIH

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00375 Urease_alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.40.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01953 Urease_alpha, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006680 Amidohydro-rel
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR011612 Urease_alpha_N_dom
IPR017950 Urease_AS
IPR005848 Urease_asu
IPR017951 Urease_asu_c
IPR029754 Urease_Ni-bd

The PANTHER Classification System

More...
PANTHERi
PTHR43440 PTHR43440, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01979 Amidohydro_1, 1 hit
PF00449 Urease_alpha, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01752 UREASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51338 SSF51338, 2 hits
SSF51556 SSF51556, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01792 urease_alph, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01120 UREASE_1, 1 hit
PS00145 UREASE_2, 1 hit
PS51368 UREASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P69996-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKISRKEYV SMYGPTTGDK VRLGDTDLIA EVEHDYTIYG EELKFGGGKT
60 70 80 90 100
LREGMSQSNN PSKEELDLII TNALIVDYTG IYKADIGIKD GKIAGIGKGG
110 120 130 140 150
NKDMQDGVKN NLSVGPATEA LAGEGLIVTA GGIDTHIHFI SPQQIPTAFA
160 170 180 190 200
SGVTTMIGGG TGPADGTNAT TITPGRRNLK WMLRAAEEYS MNLGFLAKGN
210 220 230 240 250
ASNDASLADQ IEAGAIGFKI HEDWGTTPSA INHALDVADK YDVQVAIHTD
260 270 280 290 300
TLNEAGCVED TMAAIAGRTM HTFHTEGAGG GHAPDIIKVA GEHNILPAST
310 320 330 340 350
NPTIPFTVNT EAEHMDMLMV CHHLDKSIKE DVQFADSRIR PQTIAAEDTL
360 370 380 390 400
HDMGIFSITS SDSQAMGRVG EVITRTWQTA DKNKKEFGRL KEEKGDNDNF
410 420 430 440 450
RIKRYLSKYT INPAIAHGIS EYVGSVEVGK VADLVLWSPA FFGVKPNMII
460 470 480 490 500
KGGFIALSQM GDANASIPTP QPVYYREMFA HHGKAKYDAN ITFVSQAAYD
510 520 530 540 550
KGIKEELGLE RQVLPVKNCR NITKKDMQFN DTTAHIEVNP ETYHVFVDGK
560
EVTSKPANKV SLAQLFSIF
Length:569
Mass (Da):61,684
Last modified:January 4, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4C8A6BC6C8295584
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti10V → A in CAA34933 (PubMed:2326167).Curated1
Sequence conflicti19D → A (PubMed:2326167).Curated1
Sequence conflicti22R → C AA sequence (PubMed:1857197).Curated1
Sequence conflicti27D → C AA sequence (PubMed:1857197).Curated1
Sequence conflicti104M → T in CAA34933 (PubMed:2326167).Curated1
Sequence conflicti181W → F in CAA34933 (PubMed:2326167).Curated1
Sequence conflicti193L → F in CAA34933 (PubMed:2326167).Curated1
Sequence conflicti218F → L in CAA34933 (PubMed:2326167).Curated1
Sequence conflicti273F → Y in CAA34933 (PubMed:2326167).Curated1
Sequence conflicti540P → S in CAA34933 (PubMed:2326167).Curated1
Sequence conflicti554 – 569SKPAN…LFSIF → LNQPIK in CAA34933 (PubMed:2326167).CuratedAdd BLAST16

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M60398 Genomic DNA Translation: AAA25021.1
X17079 Genomic DNA Translation: CAA34933.1
AE000511 Genomic DNA Translation: AAD07143.1
M84338 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
B38537 URKCBP

NCBI Reference Sequences

More...
RefSeqi
NP_206872.1, NC_000915.1
WP_000724295.1, NC_018939.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAD07143; AAD07143; HP_0072

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
899104

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
heo:C694_00350
hpy:HP0072

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|85962.47.peg.76

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

Going unnoticed - Issue 95 of June 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60398 Genomic DNA Translation: AAA25021.1
X17079 Genomic DNA Translation: CAA34933.1
AE000511 Genomic DNA Translation: AAD07143.1
M84338 Genomic DNA No translation available.
PIRiB38537 URKCBP
RefSeqiNP_206872.1, NC_000915.1
WP_000724295.1, NC_018939.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E9YX-ray3.00B1-569[»]
1E9ZX-ray3.00B1-569[»]
ProteinModelPortaliP69996
SMRiP69996
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP69996, 13 interactors
MINTiP69996
STRINGi85962.HP0072

Chemistry databases

ChEMBLiCHEMBL3885651

Protein family/group databases

MEROPSiM38.982

Proteomic databases

PaxDbiP69996

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD07143; AAD07143; HP_0072
GeneIDi899104
KEGGiheo:C694_00350
hpy:HP0072
PATRICifig|85962.47.peg.76

Phylogenomic databases

eggNOGiENOG4105CQM Bacteria
COG0804 LUCA
KOiK01428
OMAiGFDSHIH

Enzyme and pathway databases

UniPathwayi
UPA00258;UER00370

BioCyciHPY:HP0072-MONOMER
SABIO-RKiP69996

Miscellaneous databases

EvolutionaryTraceiP69996

Family and domain databases

CDDicd00375 Urease_alpha, 1 hit
Gene3Di2.30.40.10, 1 hit
HAMAPiMF_01953 Urease_alpha, 1 hit
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR011612 Urease_alpha_N_dom
IPR017950 Urease_AS
IPR005848 Urease_asu
IPR017951 Urease_asu_c
IPR029754 Urease_Ni-bd
PANTHERiPTHR43440 PTHR43440, 1 hit
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
PF00449 Urease_alpha, 1 hit
PRINTSiPR01752 UREASE
SUPFAMiSSF51338 SSF51338, 2 hits
SSF51556 SSF51556, 1 hit
TIGRFAMsiTIGR01792 urease_alph, 1 hit
PROSITEiView protein in PROSITE
PS01120 UREASE_1, 1 hit
PS00145 UREASE_2, 1 hit
PS51368 UREASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiURE1_HELPY
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P69996
Secondary accession number(s): P14917, Q9R3B3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: December 5, 2018
This is version 108 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  5. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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