P18315 (URE2_ENTAE) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Enterobacter aerogenes (Aerobacter aerogenes)

Taxonomic identifier

548 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter

Protein attributes

Sequence length	106 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Urea + H2O = CO2 + 2 NH3. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Enzyme regulation	The apoenzyme can be activated in vitro in the presence of nickel ions and carbon dioxide, which promotes carbamylation of 'Lys-217' of the UreC (alpha) subunit. Ref.6 Ref.7 Ref.8 Ref.9
Pathway	Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP-Rule MF_01954
Subunit structure	Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme. The apoenzyme interacts with an accessory complex composed of UreD, UreF and UreG, which is required for the assembly of the nickel containing metallocenter of UreC. The UreE protein may also play a direct role as a metallochaperone in nickel transfer to the urease apoprotein. Ref.4 Ref.5 Ref.7 Ref.8 Ref.11
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the urease beta subunit family.
Biophysicochemical properties	Kinetic parameters: KM=2.3 mM for urea Ref.2 Ref.3 Ref.10 Ref.18 Vmax=1.9 mmol/min/mg enzyme pH dependence: Optimum pH is 7.75.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	urea catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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 – 106

106

Urease subunit beta HAMAP-Rule MF_01954

PRO_0000067577

Experimental info

Mutagenesis

39

1

H → A: Reduces activity by 20% and reduces thermal stability above 50 degrees Celsius. Ref.3

Mutagenesis

41

1

H → A: Reduces activity by 30% and reduces thermal stability above 50 degrees Celsius. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

106

Helix Strand Turn

Details...

Beta strand

11 – 14

4

Beta strand

21 – 28

8

Beta strand

30 – 32

3

Beta strand

34 – 37

4

Helix

42 – 44

3

Beta strand

49 – 51

3

Turn

53 – 58

6

Beta strand

59 – 61

3

Beta strand

68 – 71

4

Beta strand

76 – 83

8

Sequences

	Sequence		Length	Mass (Da)
	P18315 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: A232BFCD74864EA6	FASTA	106	11,695
	10 20 30 40 50 60 MIPGEYHVKP GQIALNTGRA TCRVVVENHG DRPIQVGSHY HFAEVNPALK FDRQQAAGYR 70 80 90 100 LNIPAGTAVR FEPGQKREVE LVAFAGHRAV FGFRGEVMGP LEVNDE

References

[1]	"Sequence of the Klebsiella aerogenes urease genes and evidence for accessory proteins facilitating nickel incorporation." Mulrooney S.B., Hausinger R.P. J. Bacteriol. 172:5837-5843(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY. Strain: CG253.
[2]	"Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease." Martin P.R., Hausinger R.P. J. Biol. Chem. 267:20024-20027(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"Site-directed mutagenesis of Klebsiella aerogenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding, and catalysis." Park I.-S., Hausinger R.P. Protein Sci. 2:1034-1041(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-39 AND HIS-41.
[4]	"In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly." Park I.-S., Carr M.B., Hausinger R.P. Proc. Natl. Acad. Sci. U.S.A. 91:3233-3237(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREA; UREC AND URED.
[5]	"Evidence for the presence of urease apoprotein complexes containing UreD, UreF, and UreG in cells that are competent for in vivo enzyme activation." Park I.-S., Hausinger R.P. J. Bacteriol. 177:1947-1951(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREA; UREC; URED; UREF AND UREG.
[6]	"Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter." Park I.-S., Hausinger R.P. Science 267:1156-1158(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
[7]	"Purification and activation properties of UreD-UreF-urease apoprotein complexes." Moncrief M.B.C., Hausinger R.P. J. Bacteriol. 178:5417-5421(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREA; UREC; URED AND UREF.
[8]	"GTP-dependent activation of urease apoprotein in complex with the UreD, UreF, and UreG accessory proteins." Soriano A., Hausinger R.P. Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREA; UREC; URED; UREF AND UREG.
[9]	"UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-urease apoprotein complex." Soriano A., Colpas G.J., Hausinger R.P. Biochemistry 39:12435-12440(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, ACTIVATION OF THE APOPROTEIN BY UREE.
[10]	"Dual effects of ionic strength on Klebsiella aerogenes urease: pH-dependent activation and inhibition." Mulrooney S.B., Zakharian T., Schaller R.A., Hausinger R.P. Arch. Biochem. Biophys. 394:280-282(2001) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[11]	"Chemical cross-linking and mass spectrometric identification of sites of interaction for UreD, UreF, and urease." Chang Z., Kuchar J., Hausinger R.P. J. Biol. Chem. 279:15305-15313(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UREA; UREC; URED AND UREF, MASS SPECTROMETRY.
[12]	"The crystal structure of urease from Klebsiella aerogenes." Jabri E., Carr M.B., Hausinger R.P., Karplus P.A. Science 268:998-1004(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
[13]	"Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants." Jabri E., Karplus P.A. Biochemistry 35:10616-10626(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
[14]	"Characterization of the mononickel metallocenter in H134A mutant urease." Park I.-S., Michel L.O., Pearson M.A., Jabri E., Karplus P.A., Wang S., Dong J., Scott R.A., Koehler B.P., Johnson M.K., Hausinger R.P. J. Biol. Chem. 271:18632-18637(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA AND UREC.
[15]	"Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease." Pearson M.A., Michel L.O., Hausinger R.P., Karplus P.A. Biochemistry 36:8164-8172(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREA; UREC AND ACETOHYDROXAMIC ACID.
[16]	"Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand." Pearson M.A., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P. Biochemistry 37:6214-6220(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA; UREC AND FORMATE.
[17]	"Characterization of metal-substituted Klebsiella aerogenes urease." Yamaguchi K., Cosper N.J., Staalhandske C., Scott R.A., Pearson M.A., Karplus P.A., Hausinger R.P. J. Biol. Inorg. Chem. 4:468-477(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA AND UREC.
[18]	"Kinetic and structural characterization of urease active site variants." Pearson M.A., Park I.-S., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P. Biochemistry 39:8575-8584(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-101 IN COMPLEX WITH UREA AND UREC, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M36068 Genomic DNA. Translation: AAA25150.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A5K	X-ray	2.20	B	1-101	[»]
1A5L	X-ray	2.20	B	1-101	[»]
1A5M	X-ray	2.00	B	1-101	[»]
1A5N	X-ray	2.40	B	1-101	[»]
1A5O	X-ray	2.50	B	1-101	[»]
1EF2	X-ray	2.50	B	1-101	[»]
1EJR	X-ray	2.00	B	1-101	[»]
1EJS	X-ray	2.00	B	1-101	[»]
1EJT	X-ray	2.00	B	1-101	[»]
1EJU	X-ray	2.00	B	1-101	[»]
1EJV	X-ray	2.40	B	1-101	[»]
1EJW	X-ray	1.90	B	1-101	[»]
1EJX	X-ray	1.60	B	1-101	[»]
1FWA	X-ray	2.00	B	1-106	[»]
1FWB	X-ray	2.00	B	1-106	[»]
1FWC	X-ray	2.00	B	1-106	[»]
1FWD	X-ray	2.00	B	1-106	[»]
1FWE	X-ray	2.00	B	1-106	[»]
1FWF	X-ray	2.00	B	1-106	[»]
1FWG	X-ray	2.00	B	1-106	[»]
1FWH	X-ray	2.00	B	1-106	[»]
1FWI	X-ray	2.00	B	1-106	[»]
1FWJ	X-ray	2.20	B	1-106	[»]
1KRA	X-ray	2.30	B	1-106	[»]
1KRB	X-ray	2.50	B	1-106	[»]
1KRC	X-ray	2.50	B	1-106	[»]
2KAU	X-ray	2.00	B	1-106	[»]
4EP8	X-ray	1.55	B	1-101	[»]
4EPB	X-ray	1.75	B	1-101	[»]
4EPD	X-ray	1.70	B	1-101	[»]
4EPE	X-ray	2.05	B	1-101	[»]

ProteinModelPortal

P18315.

SMR

P18315. Positions 1-101.

ModBase

Search...

Protein-protein interaction databases

IntAct

P18315. 2 interactions.

Protein family/group databases

MEROPS

M38.982.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P18315.

UniPathway

UPA00258; UER00370.

Family and domain databases

Gene3D

2.10.150.10. 1 hit.

HAMAP

MF_01954. Urease_beta.

InterPro

IPR002019. Urease_beta.
[Graphical view]

Pfam

PF00699. Urease_beta. 1 hit.
[Graphical view]

SUPFAM

SSF51278. Urease_beta. 1 hit.

TIGRFAMs

TIGR00192. urease_beta. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P18315.

Entry information

Entry name

URE2_ENTAE

Accession

Primary (citable) accession number: P18315

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program