ID   UREG_RHOOB              Reviewed;         228 AA.
AC   C1AXZ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=ROP_57420;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC       metallocenter. This process requires GTP hydrolysis, probably
CC       effectuated by UreG. {ECO:0000255|HAMAP-Rule:MF_01389}.
CC   -!- SUBUNIT: Homodimer. UreD, UreF and UreG form a complex that acts as a
CC       GTP-hydrolysis-dependent molecular chaperone, activating the urease
CC       apoprotein by helping to assemble the nickel containing metallocenter
CC       of UreC. The UreE protein probably delivers the nickel.
CC       {ECO:0000255|HAMAP-Rule:MF_01389}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01389}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01389}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP011115; BAH53989.1; -; Genomic_DNA.
DR   RefSeq; WP_015889483.1; NC_012522.1.
DR   AlphaFoldDB; C1AXZ4; -.
DR   SMR; C1AXZ4; -.
DR   STRING; 632772.ROP_57420; -.
DR   KEGG; rop:ROP_57420; -.
DR   PATRIC; fig|632772.20.peg.5996; -.
DR   HOGENOM; CLU_072144_1_0_11; -.
DR   OrthoDB; 9802035at2; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd05540; UreG; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00101; ureG; 1.
DR   PANTHER; PTHR31715; UREASE ACCESSORY PROTEIN G; 1.
DR   PANTHER; PTHR31715:SF0; UREASE ACCESSORY PROTEIN G; 1.
DR   Pfam; PF02492; cobW; 1.
DR   PIRSF; PIRSF005624; Ni-bind_GTPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; GTP-binding; Nickel insertion; Nucleotide-binding.
FT   CHAIN           1..228
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_1000184268"
FT   BINDING         34..41
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   228 AA;  24383 MW;  4C55E005AFAAD32E CRC64;
     MPPHFIDGEP HDHHHDRPRR VRVAGEPVRI GIGGPVGSGK TALVAALCRQ LREELSLAVL
     TNDIYTTEDA DFLRRHAVLP DERIAAVQTG GCPHTAIRDD ITANLDAIDD LIAANPPLDL
     ILVESGGDNL TATFSSGLID VQIFVVDVAG GDKVPRKGGP GVTFSDLLVI NKTDLAPMVG
     ADLAVMRRDA EQVREGRPTA LISLTEDPSS GPALAWVREQ VRILADVH
//