UREG1_STRGG
ID UREG1_STRGG Reviewed; 234 AA.
AC B1W5H1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Urease accessory protein UreG 1 {ECO:0000255|HAMAP-Rule:MF_01389};
GN Name=ureG1 {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=SGR_6299;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG23128.1; -; Genomic_DNA.
DR AlphaFoldDB; B1W5H1; -.
DR SMR; B1W5H1; -.
DR STRING; 455632.SGR_6299; -.
DR PRIDE; B1W5H1; -.
DR EnsemblBacteria; BAG23128; BAG23128; SGR_6299.
DR KEGG; sgr:SGR_6299; -.
DR eggNOG; COG0378; Bacteria.
DR HOGENOM; CLU_072144_1_0_11; -.
DR OMA; VDLTIYV; -.
DR Proteomes; UP000001685; 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..234
FT /note="Urease accessory protein UreG 1"
FT /id="PRO_0000347450"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ SEQUENCE 234 AA; 24409 MW; C288FA16C98600DE CRC64;
MTRTPTGVPM HLGHTHDAPA AVSADATRPD GTRRALRIGL GGPVGSGKTA TVAALCRELR
DRLSIAVVTN DIYTREDADF LLKNAVLPPE RIQAVETGAC PHTAIRDDIS ANLEAVEDLE
DAVGPLDLIL VESGGDNLTA TFSKGLVDAQ IFVIDVAGGD DIPRKGGPGV TTADLLVVNK
TDLAPYVGSD LERMALDAKK QRGDLPVAFT SLTSAEGVGP VADWVRAQLA AWAA