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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-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Urea + H2O = CO2 + 2 NH3.UniRule annotation3 Publications

Cofactori

Ni cationNote: Binds 2 nickel ions per subunit.

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.

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 (ureB), Urease subunit beta (ureB), Urease subunit alpha (ureA), Urease (ureA)
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
Metal bindingi136Nickel 1; via tele nitrogen1
Metal bindingi138Nickel 1; via tele nitrogen1
Metal bindingi219Nickel 1; via carbamate group1
Metal bindingi219Nickel 2; via carbamate group1
Binding sitei221SubstrateCurated1
Metal bindingi248Nickel 2; via pros nitrogen1
Metal bindingi274Nickel 2; via tele nitrogen1
Active sitei322Proton donorCurated1
Metal bindingi362Nickel 11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

BioCyciHPY:HP0072-MONOMER.
UniPathwayiUPA00258; UER00370.

Protein family/group databases

MEROPSiM38.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Urease subunit betaUniRule annotation (EC:3.5.1.5UniRule annotation)
Alternative name(s):
Urea amidohydrolase subunit betaUniRule annotation
Gene namesi
Name:ureBUniRule annotation
Synonyms:hpuB
Ordered Locus Names:HP_0072
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000429 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

  • Note: Also associates with the outer membrane upon autolysis of neighboring bacteria.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells do not express urease.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000675331 – 569Urease subunit betaAdd BLAST569

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei219N6-carboxylysineUniRule annotation1 Publication1

Post-translational modificationi

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

Proteomic databases

PaxDbiP69996.

Expressioni

Inductioni

By nickel ions.2 Publications

Interactioni

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

Protein-protein interaction databases

IntActiP69996. 12 interactors.
MINTiMINT-1567059.
STRINGi85962.HP0072.

Structurei

Secondary structure

1569
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi6 – 10Combined sources5
Beta strandi20 – 22Combined sources3
Beta strandi29 – 31Combined sources3
Beta strandi49 – 53Combined sources5
Turni54 – 56Combined sources3
Beta strandi67 – 77Combined sources11
Beta strandi80 – 89Combined sources10
Beta strandi92 – 97Combined sources6
Turni102 – 104Combined sources3
Beta strandi105 – 107Combined sources3
Helixi110 – 112Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi127 – 130Combined sources4
Beta strandi132 – 138Combined sources7
Helixi144 – 150Combined sources7
Beta strandi153 – 159Combined sources7
Helixi165 – 169Combined sources5
Helixi175 – 186Combined sources12
Beta strandi189 – 198Combined sources10
Helixi204 – 212Combined sources9
Beta strandi216 – 220Combined sources5
Helixi222 – 224Combined sources3
Helixi228 – 240Combined sources13
Beta strandi244 – 247Combined sources4
Helixi258 – 265Combined sources8
Beta strandi270 – 272Combined sources3
Turni273 – 276Combined sources4
Turni283 – 285Combined sources3
Helixi286 – 291Combined sources6
Beta strandi295 – 299Combined sources5
Helixi301 – 303Combined sources3
Helixi310 – 320Combined sources11
Turni321 – 323Combined sources3
Helixi329 – 338Combined sources10
Helixi341 – 352Combined sources12
Beta strandi365 – 367Combined sources3
Helixi372 – 387Combined sources16
Beta strandi395 – 397Combined sources3
Helixi399 – 406Combined sources8
Helixi407 – 409Combined sources3
Helixi411 – 416Combined sources6
Turni420 – 422Combined sources3
Beta strandi423 – 426Combined sources4
Beta strandi434 – 437Combined sources4
Turni439 – 444Combined sources6
Beta strandi447 – 451Combined sources5
Beta strandi454 – 460Combined sources7
Beta strandi465 – 468Combined sources4
Beta strandi470 – 472Combined sources3
Beta strandi474 – 477Combined sources4
Helixi479 – 481Combined sources3
Helixi485 – 489Combined sources5
Beta strandi491 – 494Combined sources4
Helixi496 – 500Combined sources5
Helixi503 – 506Combined sources4
Beta strandi511 – 515Combined sources5
Helixi524 – 526Combined sources3
Beta strandi527 – 529Combined sources3
Beta strandi536 – 538Combined sources3
Turni540 – 542Combined sources3
Beta strandi545 – 547Combined sources3
Beta strandi561 – 563Combined sources3
Turni564 – 566Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E9YX-ray3.00B1-569[»]
1E9ZX-ray3.00B1-569[»]
ProteinModelPortaliP69996.
SMRiP69996.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69996.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini131 – 569UreaseUniRule annotationAdd BLAST439

Sequence similaritiesi

Belongs to the urease family.UniRule annotation
Contains 1 urease domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CQM. Bacteria.
COG0804. LUCA.
KOiK01428.
OMAiFDSHIHF.

Family and domain databases

CDDicd00375. Urease_alpha. 1 hit.
Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
InterProiIPR006680. 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.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSiPR01752. UREASE.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 2 hits.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
PROSITEiPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i4C8A6BC6C8295584
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
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.

Genome annotation databases

EnsemblBacteriaiAAD07143; AAD07143; HP_0072.
GeneIDi899104.
KEGGiheo:C694_00350.
hpy:HP0072.
PATRICi20591347. VBIHelPyl33062_0075.

Cross-referencesi

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

Protein-protein interaction databases

IntActiP69996. 12 interactors.
MINTiMINT-1567059.
STRINGi85962.HP0072.

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.
PATRICi20591347. VBIHelPyl33062_0075.

Phylogenomic databases

eggNOGiENOG4105CQM. Bacteria.
COG0804. LUCA.
KOiK01428.
OMAiFDSHIHF.

Enzyme and pathway databases

UniPathwayiUPA00258; UER00370.
BioCyciHPY:HP0072-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69996.

Family and domain databases

CDDicd00375. Urease_alpha. 1 hit.
Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01953. Urease_alpha. 1 hit.
InterProiIPR006680. 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.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
PF00449. Urease_alpha. 1 hit.
[Graphical view]
PRINTSiPR01752. UREASE.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 2 hits.
TIGRFAMsiTIGR01792. urease_alph. 1 hit.
PROSITEiPS01120. UREASE_1. 1 hit.
PS00145. UREASE_2. 1 hit.
PS51368. UREASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiURE1_HELPY
AccessioniPrimary (citable) accession number: P69996
Secondary accession number(s): P14917, Q9R3B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: November 2, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.