ID V9XDZ9_9NOCA Unreviewed; 208 AA.
AC V9XDZ9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Urease accessory protein UreG {ECO:0000256|HAMAP-Rule:MF_01389};
GN Name=ureG {ECO:0000256|HAMAP-Rule:MF_01389};
GN ORFNames=Y013_13885 {ECO:0000313|EMBL:AHD21666.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD21666.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD21666.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD21666.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
CC -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC metallocenter. This process requires GTP hydrolysis, probably
CC effectuated by UreG. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01389}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01389}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC subfamily. {ECO:0000256|ARBA:ARBA00005732, ECO:0000256|HAMAP-
CC Rule:MF_01389}.
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DR EMBL; CP006996; AHD21666.1; -; Genomic_DNA.
DR RefSeq; WP_024102407.1; NC_023150.1.
DR AlphaFoldDB; V9XDZ9; -.
DR GeneID; 29938509; -.
DR KEGG; rpy:Y013_13885; -.
DR PATRIC; fig|1435356.3.peg.2795; -.
DR eggNOG; COG0378; Bacteria.
DR HOGENOM; CLU_072144_1_0_11; -.
DR Proteomes; UP000018781; 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 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 {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01389};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01389};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01389};
KW Nickel insertion {ECO:0000256|ARBA:ARBA00022988, ECO:0000256|HAMAP-
KW Rule:MF_01389};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01389}.
FT DOMAIN 7..177
FT /note="CobW/HypB/UreG nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF02492"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01389"
SQ SEQUENCE 208 AA; 22219 MW; FA0F0125D60311F7 CRC64;
MTEAIRIGIG GPVGSGKTRL LERLLPKFRA AGIDIAVITN DLMTDEDAQR VRRSGLIDPQ
RVLAVETGAC PHTAIREDPS ANLTAVAHLE HSFPELQVVL IESGGDNLAA TFTSDLVDYW
IFVIDTAAGD DIPRKKGIGM LQADLLVINK IDLAPLVGAD LDRMRSDVAH ARPGKPSVFT
DLGSGTGLDE LFELIVRGAM LENMASAP
//