ID   UREG_YEREN              Reviewed;         221 AA.
AC   P42871;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389};
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A2635 / Serotype O:8;
RX   PubMed=8045421; DOI=10.1016/0378-1119(94)90318-2;
RA   de Koning-Ward T.F., Ward A.C., Robins-Browne R.M.;
RT   "Characterisation of the urease-encoding gene complex of Yersinia
RT   enterocolitica.";
RL   Gene 145:25-32(1994).
RN   [2]
RP   ROLE IN VIRULENCE.
RC   STRAIN=W22703 / Serogroup O:9;
RX   PubMed=7558281; DOI=10.1128/iai.63.10.3790-3795.1995;
RA   de Koning-Ward T.F., Robins-Browne R.M.;
RT   "Contribution of urease to acid tolerance in Yersinia enterocolitica.";
RL   Infect. Immun. 63:3790-3795(1995).
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   -!- FUNCTION: Expression of the urease operon increases the likelihood of
CC       bacterial survival by contibuting to acid resistance in vitro and in
CC       vivo in BALB/c mice. Y.enterocolitica enters the body via an oral path
CC       and must survive the acidic stomach before being able to colonize the
CC       intestinal mucosa (PubMed:7558281). {ECO:0000269|PubMed:7558281}.
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; L24101; AAA50999.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42871; -.
DR   SMR; P42871; -.
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   Virulence.
FT   CHAIN           1..221
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_0000067676"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   221 AA;  24181 MW;  BE23E166E8454529 CRC64;
     MNSHSTDKRK KITRIGIGGP VGSGKTAIIE VITPILIKRG IKPLIITNDI VTTEDAKQVK
     RTLKGILDEE KILGVETGAC PHTAVREDPS MNIAAVEEME ERFPDSNLIM IESGGDNLTL
     TFSPALADFY IYVIDVAEGE KIPRKNGPGL VQADILVINK IDLAPYVGAS LDVMESDTKV
     VRGERPYILT NCKTGQGIEE LVDMIMRDFL FTHVQPQGEH A