P41022 (URE3_BACPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Urease subunit gamma
EC=3.5.1.5

Alternative name(s):
Urea amidohydrolase subunit gamma

Gene names

Name:

ureA

Organism

Bacillus pasteurii

Taxonomic identifier

1474 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Planococcaceae › Sporosarcina

Protein attributes

Sequence length	100 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Urea + H2O = CO2 + 2 NH3. HAMAP-Rule MF_00739
Pathway	Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP-Rule MF_00739
Subunit structure	Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00739.
Post-translational modification	Although not discussed in the published references, Met-1 is represented in the submitted PDB entries as being modified by either a formyl, a carboxyl, or an acetyl group. The N-terminal is probably N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine. HAMAP-Rule MF_00739
Sequence similarities	Belongs to the urease gamma subunit family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Formylation
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	nickel cation binding Inferred from electronic annotation. Source: InterPro urease activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 100

100

Urease subunit gamma HAMAP-Rule MF_00739

PRO_0000097991

Amino acid modifications

Modified residue

1

1

N-formylmethionine Probable

Secondary structure

1

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100

Helix Strand Turn

Details...

Helix

5 – 25

21

Helix

32 – 49

18

Helix

53 – 59

7

Helix

60 – 62

3

Helix

66 – 68

3

Helix

73 – 76

4

Beta strand

78 – 86

9

Beta strand

89 – 97

9

Sequences

	Sequence		Length	Mass (Da)
	P41022 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 773EC3587BF6CA36	FASTA	100	11,146
	10 20 30 40 50 60 MHLNPAEKEK LQIFLASELL LRRKARGLKL NYPEAVAIIT SFIMEGARDG KTVAMLMEEG 70 80 90 100 KHVLTRDDVM EGVPEMIDDI QAEATFPDGT KLVTVHNPIS

References

[1]	"Nucleotide sequence of three genes on a urease encoding DNA-fragment from Bacillus pasteurii." Moersdorf G., Weinmann P., Kaltwasser H. Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
[2]	"Crystallization and preliminary high-resolution X-ray diffraction analysis of native and beta-mercaptoethanol-inhibited urease from Bacillus pasteurii." Benini S., Ciurli S., Rypniewski W.R., Wilson K.S., Mangani S. Acta Crystallogr. D 54:409-412(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND BETA-MERCAPTOETHANOL.
[3]	"A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels." Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S. Structure 7:205-216(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND DIAMIDOPHOSPHATE.
[4]	"The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution." Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S. J. Biol. Inorg. Chem. 5:110-118(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND ACETOHYDROXAMIC ACID.
[5]	"Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism." Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S. J. Biol. Inorg. Chem. 6:778-790(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND PHOSPHATE.
[6]	"Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism." Benini S., Rypniewski W.R., Wilson K.S., Mangani S., Ciurli S. J. Am. Chem. Soc. 126:3714-3715(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND BORATE IONS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X78411 Genomic DNA. Translation: CAA55173.1.

PIR

S47102.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IE7	X-ray	1.85	A	1-100	[»]
1S3T	X-ray	2.10	A	1-100	[»]
1UBP	X-ray	1.65	A	1-100	[»]
2UBP	X-ray	2.00	A	1-100	[»]
3UBP	X-ray	2.00	A	1-100	[»]
4AC7	X-ray	1.50	A	1-100	[»]
4UBP	X-ray	1.55	A	1-100	[»]

ProteinModelPortal

P41022.

SMR

P41022. Positions 1-100.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00258; UER00370.

Family and domain databases

Gene3D

3.30.280.10. 1 hit.

HAMAP

MF_00739. Urease_gamma.

InterPro

IPR002026. Urease_gamma/gamma-beta_su.
IPR012010. Urease_gamma_su.
[Graphical view]

Pfam

PF00547. Urease_gamma. 1 hit.
[Graphical view]

PIRSF

PIRSF001223. Urease_gamma. 1 hit.

ProDom

PD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF54111. Urease_gamma_reg. 1 hit.

TIGRFAMs

TIGR00193. urease_gam. 1 hit.

ProtoNet

Search...

Other

BindingDB

P41022.

EvolutionaryTrace

P41022.

Entry information

Entry name

URE3_BACPA

Accession

Primary (citable) accession number: P41022

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program