UREG_SPOPA
ID UREG_SPOPA Reviewed; 211 AA.
AC Q9RP19; Q45346;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Urease accessory protein UreG;
GN Name=ureG;
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX PubMed=12072968; DOI=10.1007/s00775-002-0341-7;
RA Ciurli S., Safarov N., Miletti S., Dikiy A., Christensen S.K.,
RA Kornetzky K., Bryant D.A., Vandenberghe I., Devreese B., Samyn B.,
RA Remaut H., Van Beeumen J.;
RT "Molecular characterization of Bacillus pasteurii UreE, a metal-binding
RT chaperone for the assembly of the urease active site.";
RL J. Biol. Inorg. Chem. 7:623-631(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-210.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RA You J.-H., Kim J.-G., Song B.-H., Lee M.-H., Kim S.-D.;
RT "Genetic organization and nucleotide sequence of the ure gene cluster in
RT Bacillus pasteurii.";
RL Mol. Cells 5:359-369(1995).
RN [3]
RP PROTEIN SEQUENCE OF 1-6 AND 209-211, MASS SPECTROMETRY, SUBUNIT, GTPASE
RP ACTIVITY, ZINC AND NICKEL-BINDING, FUNCTION, DOMAIN, AND MODELING.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX PubMed=15542602; DOI=10.1074/jbc.m408483200;
RA Zambelli B., Stola M., Musiani F., De Vriendt K., Samyn B., Devreese B.,
RA Van Beeumen J., Turano P., Dikiy A., Bryant D.A., Ciurli S.;
RT "UreG, a chaperone in the urease assembly process, is an intrinsically
RT unstructured GTPase that specifically binds Zn2+.";
RL J. Biol. Chem. 280:4684-4695(2005).
RN [4]
RP FOLDING STUDIES, DOMAIN, SUBUNIT, AND DISULFIDE BOND.
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX PubMed=16846235; DOI=10.1021/bi060227s;
RA Neyroz P., Zambelli B., Ciurli S.;
RT "Intrinsically disordered structure of Bacillus pasteurii UreG as revealed
RT by steady-state and time-resolved fluorescence spectroscopy.";
RL Biochemistry 45:8918-8930(2006).
CC -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC metallocenter. Binds a maximum of 4 Ni(2+) and 2 Zn(2+) ions per
CC homodimer. The affinity for Zn(2+) is 10-fold higher than that for
CC Ni(2+). This process requires GTP hydrolysis.
CC {ECO:0000269|PubMed:15542602}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. The physiological role of the
CC disulfide bond has not been proven in vivo. UreD, UreF and UreG form a
CC complex that acts as a GTP-hydrolysis-dependent molecular chaperone,
CC activating the urease apoprotein by helping to assemble the nickel-
CC containing metallocenter. {ECO:0000269|PubMed:15542602,
CC ECO:0000269|PubMed:16846235}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Exists in a relatively unstructured form; binding to the other
CC subunits (UreD, UreF and apourease) may induce correct protein folding.
CC The presence of Zn2(+) or GTP does not alter the unfolded state.
CC {ECO:0000269|PubMed:15542602, ECO:0000269|PubMed:16846235}.
CC -!- MASS SPECTROMETRY: Mass=23084.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15542602};
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC subfamily. {ECO:0000305}.
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DR EMBL; AF361945; AAD55060.1; -; Genomic_DNA.
DR EMBL; U29368; AAA73989.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RP19; -.
DR SMR; Q9RP19; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IDA:CAFA.
DR GO; GO:0003924; F:GTPase activity; IDA:CAFA.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0016151; F:nickel cation binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01389; UreG; 1.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004400; UreG.
DR PANTHER; PTHR31715; PTHR31715; 1.
DR Pfam; PF02492; cobW; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00101; ureG; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW GTP-binding; Nickel insertion; Nucleotide-binding.
FT CHAIN 1..211
FT /note="Urease accessory protein UreG"
FT /id="PRO_0000347347"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT DISULFID 68
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:16846235"
FT CONFLICT 100..186
FT /note="Missing (in Ref. 2; AAA73989)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..210
FT /note="ES -> RV (in Ref. 2; AAA73989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 23084 MW; E31E9913D5E4BB91 CRC64;
MKTIHLGIGG PVGSGKTTLV KTLSEALKEE YSIAVITNDI YTREDANFLI NENILEKDRI
IGVETGGCPH TAIREDASMN FEAIEELKNR FDDLEIILLE SGGDNLSATF SPELVDAFIY
VIDVSEGGDI PRKGGPGVTR SDFLMVNKTE LAPYVGVDLD TMKNDTIKAR NGRPFTFANI
KTKKGLDEII AWIKSDLLLE GKTNESASES K
