UREG_PSEPG
ID UREG_PSEPG Reviewed; 207 AA.
AC B0KUZ3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389};
GN OrderedLocusNames=PputGB1_2931;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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}.
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DR EMBL; CP000926; ABY98825.1; -; Genomic_DNA.
DR RefSeq; WP_010953755.1; NC_010322.1.
DR AlphaFoldDB; B0KUZ3; -.
DR SMR; B0KUZ3; -.
DR STRING; 76869.PputGB1_2931; -.
DR EnsemblBacteria; ABY98825; ABY98825; PputGB1_2931.
DR GeneID; 58530799; -.
DR GeneID; 66677720; -.
DR KEGG; ppg:PputGB1_2931; -.
DR eggNOG; COG0378; Bacteria.
DR HOGENOM; CLU_072144_1_0_6; -.
DR OMA; VDLTIYV; -.
DR Proteomes; UP000002157; 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; -; 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 3: Inferred from homology;
KW Chaperone; Cytoplasm; GTP-binding; Nickel insertion; Nucleotide-binding.
FT CHAIN 1..207
FT /note="Urease accessory protein UreG"
FT /id="PRO_0000347426"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ SEQUENCE 207 AA; 22449 MW; 656E150493214FA2 CRC64;
MQSYQQPLRV GVGGPVGSGK TALLEALCKA MRDHYQIAVV TNDIYTKEDQ RILTEAGALE
PERIVGVETG GCPHTAIRED ASMNLAAVEA LARKFGNLEV IFVESGGDNL SATFSPELAD
LTIYVIDVAE GEKIPRKGGP GITKSDFLVI NKTDLAPYVG ASLEVMERDT QRMRPQRPWT
FSNLKKGEGL QAVIDFIVER GMLGVRG