ID   UREG2_METRJ             Reviewed;         208 AA.
AC   B1M9D7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Urease accessory protein UreG 2 {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG2 {ECO:0000255|HAMAP-Rule:MF_01389};
GN   OrderedLocusNames=Mrad2831_6188;
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OG   Plasmid pMRAD01.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of plasmid1 of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-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; CP001002; ACB28112.1; -; Genomic_DNA.
DR   RefSeq; WP_012329898.1; NC_010510.1.
DR   AlphaFoldDB; B1M9D7; -.
DR   SMR; B1M9D7; -.
DR   STRING; 426355.Mrad2831_6188; -.
DR   PRIDE; B1M9D7; -.
DR   EnsemblBacteria; ACB28112; ACB28112; Mrad2831_6188.
DR   KEGG; mrd:Mrad2831_6188; -.
DR   eggNOG; COG0378; Bacteria.
DR   HOGENOM; CLU_072144_1_0_5; -.
DR   OMA; PHFHADE; -.
DR   OrthoDB; 1134430at2; -.
DR   Proteomes; UP000006589; Plasmid pMRAD01.
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;
KW   Plasmid; Reference proteome.
FT   CHAIN           1..208
FT                   /note="Urease accessory protein UreG 2"
FT                   /id="PRO_0000347407"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   208 AA;  21823 MW;  189C786CC0D67968 CRC64;
     MTDVTPANAA RIGIGGPVGS GKTALIERLI PVLQARGVDL AVITNDLVTK EDAERLRRSG
     LIDPSRVEAV EAGACPHTVI REDPTLNIAA GDALEARFPG LQLLVFESGG DNLASTFSLD
     LVDWWIFVID VAGGDDIPRK RGPGVLRCDL LVINKIDLAP HVGVDLEGML AEAARVRGGK
     PVIATNARAG LGIDRVADAI GRAVLFTP