ID   UREG_KLEAE              Reviewed;         205 AA.
AC   P18319;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389};
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CG253;
RX   PubMed=2211515; DOI=10.1128/jb.172.10.5837-5843.1990;
RA   Mulrooney S.B., Hausinger R.P.;
RT   "Sequence of the Klebsiella aerogenes urease genes and evidence for
RT   accessory proteins facilitating nickel incorporation.";
RL   J. Bacteriol. 172:5837-5843(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-5.
RX   PubMed=1624427; DOI=10.1128/jb.174.13.4324-4330.1992;
RA   Lee M.H., Mulrooney S.B., Renner M.J., Markowicz Y., Hausinger R.P.;
RT   "Klebsiella aerogenes urease gene cluster: sequence of ureD and
RT   demonstration that four accessory genes (ureD, ureE, ureF, and ureG) are
RT   involved in nickel metallocenter biosynthesis.";
RL   J. Bacteriol. 174:4324-4330(1992).
RN   [3]
RP   SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-20 AND
RP   THR-21.
RX   PubMed=9209019; DOI=10.1128/jb.179.13.4081-4086.1997;
RA   Moncrief M.B.C., Hausinger R.P.;
RT   "Characterization of UreG, identification of a UreD-UreF-UreG complex, and
RT   evidence suggesting that a nucleotide-binding site in UreG is required for
RT   in vivo metallocenter assembly of Klebsiella aerogenes urease.";
RL   J. Bacteriol. 179:4081-4086(1997).
RN   [4]
RP   COMPLEX FORMATION, GTP HYDROLYSIS, AND INTERACTION WITH UREA; UREB; UREC;
RP   URED AND UREF.
RX   PubMed=10500143; DOI=10.1073/pnas.96.20.11140;
RA   Soriano A., Hausinger R.P.;
RT   "GTP-dependent activation of urease apoprotein in complex with the UreD,
RT   UreF, and UreG accessory proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999).
CC   -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC       metallocenter. This process requires GTP hydrolysis, probably
CC       effectuated by UreG.
CC   -!- ACTIVITY REGULATION: Activation of apourease within the UreDFG-
CC       apoprotein complex is inhibited by zinc, copper and cobalt.
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   -!- INTERACTION:
CC       P18319; Q09063: ureD; NbExp=4; IntAct=EBI-6410613, EBI-6410589;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01389,
CC       ECO:0000269|PubMed:9209019}.
CC   -!- MASS SPECTROMETRY: Mass=21814; Mass_error=20; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9209019};
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; M36068; AAA25154.1; -; Genomic_DNA.
DR   RefSeq; WP_002916877.1; NZ_LR134254.1.
DR   AlphaFoldDB; P18319; -.
DR   SMR; P18319; -.
DR   IntAct; P18319; 1.
DR   GeneID; 61334826; -.
DR   GeneID; 64293491; -.
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; Direct protein sequencing; GTP-binding;
KW   Nickel insertion; Nucleotide-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..205
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_0000067666"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         20
FT                   /note="K->A: Does not produce active urease, no UreDFG-
FT                   apourease complexes are formed."
FT                   /evidence="ECO:0000269|PubMed:9209019"
FT   MUTAGEN         21
FT                   /note="T->A: Does not produce active urease, no UreDFG-
FT                   apourease complexes are formed."
FT                   /evidence="ECO:0000269|PubMed:9209019"
SQ   SEQUENCE   205 AA;  21944 MW;  79BE91D1DEE90A81 CRC64;
     MNSYKHPLRV GVGGPVGSGK TALLEALCKA MRDTWQLAVV TNDIYTKEDQ RILTEAGALA
     PERIVGVETG GCPHTAIRED ASMNLAAVEA LSEKFGNLDL IFVESGGDNL SATFSPELAD
     LTIYVIDVAE GEKIPRKGGP GITKSDFLVI NKTDLAPYVG ASLEVMASDT QRMRGDRPWT
     FTNLKQGDGL STIIAFLEDK GMLGK