ID   UREG_STRE5              Reviewed;         204 AA.
AC   Q55057; F8HGJ7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=Ssal_01896;
OS   Streptococcus salivarius (strain 57.I).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1046629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=57.I;
RX   PubMed=8550211; DOI=10.1128/iai.64.2.585-592.1996;
RA   Chen Y.-Y.M., Clancy K.A., Burne R.A.;
RT   "Streptococcus salivarius urease: genetic and biochemical characterization
RT   and expression in a dental plaque streptococcus.";
RL   Infect. Immun. 64:585-592(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=57.I;
RX   PubMed=21914897; DOI=10.1128/jb.05670-11;
RA   Geng J., Huang S.C., Li S., Hu S., Chen Y.Y.;
RT   "Complete genome sequence of the ureolytic Streptococcus salivarius strain
RT   57.I.";
RL   J. Bacteriol. 193:5596-5597(2011).
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; U35248; AAC43567.1; -; Genomic_DNA.
DR   EMBL; CP002888; AEJ54133.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q55057; -.
DR   SMR; Q55057; -.
DR   STRING; 1046629.Ssal_01896; -.
DR   EnsemblBacteria; AEJ54133; AEJ54133; Ssal_01896.
DR   KEGG; stf:Ssal_01896; -.
DR   PATRIC; fig|1046629.4.peg.1683; -.
DR   eggNOG; COG0378; Bacteria.
DR   OMA; VDLTIYV; -.
DR   Proteomes; UP000000293; 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..204
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_0000067673"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   204 AA;  22942 MW;  51303ECAFECD892A CRC64;
     MTKRTVIIGV GGPVGSGKTL LLERLTRRMS DLNLAVITND IYTKEDALFL AKNSSLDEDR
     IIGVETGGCP HTAIREDASM NFEAIETLQE RFNHDLDVIF LESGGDNLAA TFSPDLVDFT
     IYIIDVAQGE KIPRKAGQGM IKSDLFLINK TDLAPYVGAN LDRMREDTLH FRNEDSFIFT
     NLNNDDNVKE VEEWIRKNFL LEDL