Reviewed, UniProtKB/Swiss-Prot P69997 (URE1_HELPJ)

Names and origin

Protein names

Recommended name:
    Urease subunit beta
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit beta

Gene names

Name:	ureB
Synonyms:	hpuB
Ordered Locus Names:	jhp_0067

Organism

Helicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP]

Taxonomic identifier

85963 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	569 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach By similarity.
Catalytic activity	Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953
Cofactor	Binds 2 nickel ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953
Subunit structure	Heterohexamer of 3 ureA (alpha) and 3 ureB (beta) subunits. Four heterohexamers assemble to form a 16 nm dodecameric complex By similarity.
Subcellular location	Cytoplasm. Note: Also associates with the outer membrane upon autolysis of neighboring bacteria By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two nickel ions By similarity.
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 By similarity.
Sequence similarities	Belongs to the urease family. Contains 1 urease domain.
Caution	The orthologous protein is known as the alpha subunit (ureC) in most other bacteria.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Nickel
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	urea metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW urease activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 569	569	Urease subunit beta HAMAP MF_01953		PRO_0000067534
Regions
	Domain	131 – 569	439	Urease
Sites
	Active site	322	1	Proton donor By similarity
	Metal binding	136	1	Nickel 2 By similarity
	Metal binding	138	1	Nickel 2 By similarity
	Metal binding	219	1	Nickel 1; via carbamate group By similarity
	Metal binding	219	1	Nickel 2; via carbamate group By similarity
	Metal binding	248	1	Nickel 1 By similarity
	Metal binding	274	1	Nickel 1 By similarity
	Metal binding	362	1	Nickel 2 By similarity
	Binding site	221	1	Substrate By similarity
Amino acid modifications
	Modified residue	219	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P69997-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 4C8A6BC6C8295584	FASTA	569	61,684
	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

References

[1]

"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J. Nature 397:176-180(1999) [PubMed: 9923682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE001439 Genomic DNA. Translation: AAD05651.1.
PIR	URKCBP. B38537.
RefSeq	NP_222789.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P69997.
Genome annotation databases
GeneID	890410.
GenomeReviews	Gene locus jhp_0067 in contig AE001439_GR.
KEGG	hpj:jhp0067.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P69997.
OMA	SHIHFIC.
Enzyme and pathway databases
BioCyc	HPYL85963:JHP0067-MON.
BRENDA	3.5.1.5. 295085.
Family and domain databases
HAMAP	MF_01953. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR011612. Urease_alpha_N. IPR005848. Urease_asu. IPR017951. Urease_asu_c. IPR017952. Urease_asu_core. IPR017950. Urease_asu_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. PF00449. Urease_alpha. 1 hit. [Graphical view]
PRINTS	PR01752. UREASE.
TIGRFAMs	TIGR01792. urease_alph. 1 hit.
PROSITE	PS01120. UREASE_1. 1 hit. PS00145. UREASE_2. 1 hit. PS51368. UREASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

URE1_HELPJ

Accession

Primary (citable) accession number: P69997
Secondary accession number(s): P14917

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)