Reviewed, UniProtKB/Swiss-Prot Q9RP19 (UREG_BACPA)

Names and origin

Protein names

Recommended name:
    Urease accessory protein ureG

Gene names

Name:

ureG

Organism

Bacillus pasteurii

Taxonomic identifier

1474 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Planococcaceae › Sporosarcina

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by ureG By similarity. HAMAP MF_01389 Exists in a relatively unstructured form; binding to the other subunits (ureD, ureF and apourease) may induce correct protein folding. The presence of Zn2+ or GTP does not alter the unfolded state. HAMAP MF_01389
Cofactor	Binds a maximum of 4 Ni2+ and 2 Zn2+ ions per homodimer. The affinity for Zn2+ is 10-fold higher than that for Ni2+. HAMAP MF_01389
Subunit structure	Homodimer; disulfide-linked. The physiological role of the disulfide bond has not been proven in vivo. Ref.3 Ref.4
Subcellular location	Cytoplasm By similarity HAMAP MF_01389.
Sequence similarities	Belongs to the ureG family.
Mass spectrometry	Molecular mass is 23084.5 Da from positions 1 - 211. Determined by ESI. Ref.3

Ontologies

Keywords
Biological process	Nickel insertion
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: UniProtKB-KW nickel ion binding 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 – 211	211	Urease accessory protein ureG HAMAP MF_01389		PRO_0000347347
Regions
	Nucleotide binding	10 – 17	8	GTP By similarity
Amino acid modifications
	Disulfide bond	68		Interchain Ref.4
Experimental info
	Sequence conflict	100 – 186	87	Missing in AAA73989. Ref.2
	Sequence conflict	209 – 210	2	ES → RV in AAA73989. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9RP19-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E31E9913D5E4BB91	FASTA	211	23,084
	10 20 30 40 50 60 MKTIHLGIGG PVGSGKTTLV KTLSEALKEE YSIAVITNDI YTREDANFLI NENILEKDRI 70 80 90 100 110 120 IGVETGGCPH TAIREDASMN FEAIEELKNR FDDLEIILLE SGGDNLSATF SPELVDAFIY 130 140 150 160 170 180 VIDVSEGGDI PRKGGPGVTR SDFLMVNKTE LAPYVGVDLD TMKNDTIKAR NGRPFTFANI 190 200 210 KTKKGLDEII AWIKSDLLLE GKTNESASES K

References

[1]	"Molecular characterization of Bacillus pasteurii UreE, a metal-binding chaperone for the assembly of the urease active site." Ciurli S., Safarov N., Miletti S., Dikiy A., Christensen S.K., Kornetzky K., Bryant D.A., Vandenberghe I., Devreese B., Samyn B., Remaut H., Van Beeumen J. J. Biol. Inorg. Chem. 7:623-631(2002) [PubMed: 12072968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
[2]	"Genetic organization and nucleotide sequence of the ure gene cluster in Bacillus pasteurii." You J.-H., Kim J.-G., Song B.-H., Lee M.-H., Kim S.-D. Mol. Cells 5:359-369(1995) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-210. Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
[3]	"UreG, a chaperone in the urease assembly process, is an intrinsically unstructured GTPase that specifically binds Zn2+." Zambelli B., Stola M., Musiani F., De Vriendt K., Samyn B., Devreese B., Van Beeumen J., Turano P., Dikiy A., Bryant D.A., Ciurli S. J. Biol. Chem. 280:4684-4695(2005) [PubMed: 15542602] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-6 AND 209-211, MASS SPECTROMETRY, SUBUNIT, GTPASE ACTIVITY, ZINC AND NICKEL-BINDING, MODELING. Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.
[4]	"Intrinsically disordered structure of Bacillus pasteurii UreG as revealed by steady-state and time-resolved fluorescence spectroscopy." Neyroz P., Zambelli B., Ciurli S. Biochemistry 45:8918-8930(2006) [PubMed: 16846235] [Abstract] Cited for: FOLDING STUDIES, DISULFIDE BOND. Strain: ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF361945 Genomic DNA. Translation: AAD55060.1. U29368 Genomic DNA. Translation: AAA73989.1.
3D structure databases
SMR	Q9RP19. Positions 5-196.
ModBase	Search...
Family and domain databases
HAMAP	MF_01389. UreG. [Tree]
InterPro	IPR003495. Cbl_biosynth_CobW-like. IPR012202. NiFe_hyd/urase_mat_GTPase. IPR004400. Urease_accessory_UreG. [Graphical view]
Pfam	PF02492. cobW. 1 hit. [Graphical view]
PIRSF	PIRSF005624. Ni-bind_GTPase. 1 hit.
TIGRFAMs	TIGR00101. ureG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

UREG_BACPA

Accession

Primary (citable) accession number: Q9RP19
Secondary accession number(s): Q45346

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
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)