ID   UREG_VIBPH              Reviewed;         212 AA.
AC   Q9FAS2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389};
OS   Vibrio parahaemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TH3996;
RX   PubMed=10992480; DOI=10.1128/iai.68.10.5742-5748.2000;
RA   Park K.-S., Iida T., Yamaichi Y., Oyagi T., Yamamoto K., Honda T.;
RT   "Genetic characterization of DNA region containing the trh and ure genes of
RT   Vibrio parahaemolyticus.";
RL   Infect. Immun. 68:5742-5748(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TH3996;
RX   PubMed=19075025; DOI=10.1128/iai.01184-08;
RA   Okada N., Iida T., Park K.-S., Goto N., Yasunaga T., Hiyoshi H.,
RA   Matsuda S., Kodama T., Honda T.;
RT   "Identification and characterization of a novel type III secretion system
RT   in trh-positive Vibrio parahaemolyticus strain TH3996 reveal genetic
RT   lineage and diversity of pathogenic machinery beyond the species level.";
RL   Infect. Immun. 77:904-913(2009).
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; AB455531; BAB13791.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9FAS2; -.
DR   SMR; Q9FAS2; -.
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..212
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_0000347456"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   212 AA;  23159 MW;  C942A2638E663C3E CRC64;
     MQEYNNQDYK QPLRIGVGGP VGSGKTALLE ILCKTIRDKY QIAVVTNDIY TQEDAKILTR
     AQALDADRII GVETGGCPHT AIREDASMNL AAVEELAKRH KNLDLVFVES GGDNLSATFS
     PELADLTIYV IDVAEGEKIP RKGGPGITRS DLLVINKIDL APYVGASLDV MEADTARMRP
     EKPYVFTNLK EGIGLQKIID FIVDKGMLPK VD