ID   UREG2_BRUO2             Reviewed;         212 AA.
AC   A5VRB1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Urease accessory protein UreG 2 {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG2 {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=BOV_1317;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
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; CP000708; ABQ60430.1; -; Genomic_DNA.
DR   RefSeq; WP_002964473.1; NC_009505.1.
DR   AlphaFoldDB; A5VRB1; -.
DR   SMR; A5VRB1; -.
DR   PRIDE; A5VRB1; -.
DR   EnsemblBacteria; ABQ60430; ABQ60430; BOV_1317.
DR   GeneID; 45124712; -.
DR   GeneID; 55591021; -.
DR   KEGG; bov:BOV_1317; -.
DR   HOGENOM; CLU_072144_1_0_5; -.
DR   OMA; TQEDAQH; -.
DR   PhylomeDB; A5VRB1; -.
DR   Proteomes; UP000006383; Chromosome I.
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..212
FT                   /note="Urease accessory protein UreG 2"
FT                   /id="PRO_0000347361"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   212 AA;  22977 MW;  C436DF98D5E8D12C CRC64;
     MKKIPRIGVG GPVGSGKTAI IEAVVPILIK LGYRILVITN DIVTTEDAKH VQRTLKGVLI
     EDRIVGVETG GCPHTAVRED PSMNLAAVEE MEAKFPDTDL VLLESGGDNL TLTFSPALID
     FFIYVIDVAA GDKIPRKNGP GISQSDILVI NKTDLAPYVG ASLQVMDDDS RMMRGKKPFV
     FTNCKTNEGI DDLVHLIREN VLFDTEVSKE SA