ID UREG_SYNY3 Reviewed; 206 AA. AC P72955; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389}; GN Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; GN OrderedLocusNames=sll0643; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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; BA000022; BAA16973.1; -; Genomic_DNA. DR PIR; S74933; S74933. DR AlphaFoldDB; P72955; -. DR SMR; P72955; -. DR STRING; 1148.gene:10497833; -. DR PaxDb; 1148-1652048; -. DR EnsemblBacteria; BAA16973; BAA16973; BAA16973. DR KEGG; syn:sll0643; -. DR eggNOG; COG0378; Bacteria. DR InParanoid; P72955; -. DR PhylomeDB; P72955; -. DR Proteomes; UP000001425; 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 CDD; cd05540; UreG; 1. 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; Cytoplasm; GTP-binding; Nickel insertion; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..206 FT /note="Urease accessory protein UreG" FT /id="PRO_0000067674" FT BINDING 12..19 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389" SQ SEQUENCE 206 AA; 22013 MW; 8A45AD507F49B1B1 CRC64; MAQTPLRIGI AGPVGSGKTA LLEALCKALR QKYQLAVVTN DIYTQEDAQF LVRAEALTPD RILGVETGGC PHTAIREDAS LNLAAIADLE ARFMPLDMVF LESGGDNLAA TFSPELVDLT LYVIDVAAGD KIPRKGGPGI TKSDLLVINK IDLAPMVGAD LGIMDRDAKK MRGEKPFVFT NLKTATGLST VVDFVEHYLP TKVLAS //