UREG_RHILO
ID UREG_RHILO Reviewed; 213 AA.
AC Q98CZ5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=mll4934;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000012; BAB51476.1; -; Genomic_DNA.
DR RefSeq; WP_010912817.1; NC_002678.2.
DR AlphaFoldDB; Q98CZ5; -.
DR SMR; Q98CZ5; -.
DR STRING; 266835.14024874; -.
DR EnsemblBacteria; BAB51476; BAB51476; BAB51476.
DR GeneID; 66680822; -.
DR KEGG; mlo:mll4934; -.
DR eggNOG; COG0378; Bacteria.
DR HOGENOM; CLU_072144_1_0_5; -.
DR OMA; VDLTIYV; -.
DR OrthoDB; 1134430at2; -.
DR Proteomes; UP000000552; 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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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..213
FT /note="Urease accessory protein UreG"
FT /id="PRO_1000145212"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ SEQUENCE 213 AA; 22892 MW; 9E94FAA5BE1EF022 CRC64;
MTQANGPLRI GIGGPVGSGK TTLTEKLCKA LRDEFSIAVV TNDIYTREDA MMLARLQALP
EDRIVGVETG GCPHTAIRED ASINLQAIAE LNRKFPDLDI IFIESGGDNL AATFSPDLAD
LTLYVISVCQ GEEIPRKGGP AITRSDFLII NKSDLAPYVN VNLDVMESDA ARMRGKRPFG
FTDLSRGKGL REVIDFIVEH GGLRVGTATS TAA