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Database: UniProt
Entry: UREG_NOCFA
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ID   UREG_NOCFA              Reviewed;         238 AA.
AC   Q5YWQ4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=NFA_25400;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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}.
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DR   EMBL; AP006618; BAD57387.1; -; Genomic_DNA.
DR   RefSeq; WP_011209072.1; NC_006361.1.
DR   AlphaFoldDB; Q5YWQ4; -.
DR   SMR; Q5YWQ4; -.
DR   STRING; 247156.NFA_25400; -.
DR   GeneID; 61133283; -.
DR   KEGG; nfa:NFA_25400; -.
DR   eggNOG; COG0378; Bacteria.
DR   HOGENOM; CLU_072144_1_0_11; -.
DR   OrthoDB; 9802035at2; -.
DR   Proteomes; UP000006820; 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;
KW   Reference proteome.
FT   CHAIN           1..238
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_1000145198"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34..41
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   238 AA;  25060 MW;  760A712536919F74 CRC64;
     MPPHLIDGEP HDHAHDRPKR QRTPGEPLRI GIGGPVGSGK TALVAALCKQ LREELSLAVL
     TNDIYTTEDA DFLRRHAVLP DERITAVQTG GCPHTAIRDD ITANLDAIDD LIAANPPLDL
     ILVESGGDNL TATFSSGLID VQIFVIDVAG GDKVPRKGGP GVTYSDLLVV NKTDLAPLVG
     ADLGVMERDA AKVRQGRPTA LISLTDDPAA TPVLAWVREQ LAAIAEADRH GAASGIAH
//
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