ID   UREG_PROMH              Reviewed;         205 AA.
AC   Q06206; B4EXN8;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=PMI3688;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8335248; DOI=10.1016/0378-1119(93)90703-6;
RA   Sriwanthana B., Island M.D., Mobley H.L.T.;
RT   "Sequence of the Proteus mirabilis urease accessory gene ureG.";
RL   Gene 129:103-106(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
RN   [3]
RP   UREASE AS A VIRULENCE FACTOR.
RX   PubMed=2180821; DOI=10.1128/iai.58.4.1120-1123.1990;
RA   Jones B.D., Lockatell C.V., Johnson D.E., Warren J.W., Mobley H.L.T.;
RT   "Construction of a urease-negative mutant of Proteus mirabilis: analysis of
RT   virulence in a mouse model of ascending urinary tract infection.";
RL   Infect. Immun. 58:1120-1123(1990).
RN   [4]
RP   PROBABLE OPERON STRUCTURE, AND MUTAGENESIS OF ILE-134.
RX   PubMed=7559355; DOI=10.1128/jb.177.19.5653-5660.1995;
RA   Island M.D., Mobley H.L.T.;
RT   "Proteus mirabilis urease: operon fusion and linker insertion analysis of
RT   ure gene organization, regulation, and function.";
RL   J. Bacteriol. 177:5653-5660(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   -!- 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; Z21940; CAA79934.1; -; Genomic_DNA.
DR   EMBL; AM942759; CAR47190.1; -; Genomic_DNA.
DR   PIR; JN0755; JN0755.
DR   RefSeq; WP_004245259.1; NC_010554.1.
DR   AlphaFoldDB; Q06206; -.
DR   SMR; Q06206; -.
DR   STRING; 529507.PMI3688; -.
DR   EnsemblBacteria; CAR47190; CAR47190; PMI3688.
DR   GeneID; 6801998; -.
DR   KEGG; pmr:PMI3688; -.
DR   eggNOG; COG0378; Bacteria.
DR   HOGENOM; CLU_072144_1_0_6; -.
DR   OMA; VDLTIYV; -.
DR   Proteomes; UP000008319; 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   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; GTP-binding; Nickel insertion; Nucleotide-binding;
KW   Reference proteome; Virulence.
FT   CHAIN           1..205
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_0000067671"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
FT   MUTAGEN         134
FT                   /note="I->IRRRI: Abrogates activity."
FT                   /evidence="ECO:0000269|PubMed:7559355"
FT   CONFLICT        122..125
FT                   /note="TIYV -> LFML (in Ref. 1; CAA79934)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145..148
FT                   /note="SDLL -> PDMM (in Ref. 1; CAA79934)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   205 AA;  22301 MW;  A9E209D9AFD75BDD CRC64;
     MQEYNQPLRI GVGGPVGSGK TALLEVLCKA MRDSYQIAVV TNDIYTQEDA KILTRAQALD
     ADRIIGVETG GCPHTAIRED ASMNLAAVEE LAMRHKNLDI VFVESGGDNL SATFSPELAD
     LTIYVIDVAE GEKIPRKGGP GITHSDLLVI NKIDLAPYVG ASLEVMEADT AKMRPVKPYV
     FTNLKEKVGL ETIIDFIIDK GMLRR