ID   UREG_MYCTO              Reviewed;         224 AA.
AC   P9WFE2; L0T828; P0A664; P50051;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=MT1900;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; disulfide-linked (Probable). The physiological role
CC       of the disulfide bond has not been proven in vivo. UreD, UreF and UreG
CC       form a complex that acts as a GTP-hydrolysis-dependent molecular
CC       chaperone, activating the urease apoprotein by helping to assemble the
CC       nickel containing metallocenter of UreC. The UreE protein probably
CC       delivers the nickel (By similarity). {ECO:0000250, ECO:0000305}.
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; AE000516; AAK46171.1; -; Genomic_DNA.
DR   PIR; D70665; D70665.
DR   RefSeq; WP_003409313.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFE2; -.
DR   SMR; P9WFE2; -.
DR   EnsemblBacteria; AAK46171; AAK46171; MT1900.
DR   KEGG; mtc:MT1900; -.
DR   PATRIC; fig|83331.31.peg.2044; -.
DR   HOGENOM; CLU_072144_1_0_11; -.
DR   Proteomes; UP000001020; 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; Disulfide bond; GTP-binding; Nickel insertion;
KW   Nucleotide-binding.
FT   CHAIN           1..224
FT                   /note="Urease accessory protein UreG"
FT                   /id="PRO_0000428554"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
FT   DISULFID        90
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   224 AA;  23348 MW;  702D613945D76BB9 CRC64;
     MATHSHPHSH TVPARPRRVR KPGEPLRIGV GGPVGSGKTA LVAALCRQLR GELSLAVLTN
     DIYTTEDADF LRTHAVLPDD RIAAVQTGGC PHTAIRDDIT ANLDAIDELM AAHDALDLIL
     VESGGDNLTA TFSSGLVDAQ IFVIDVAGGD KVPRKGGPGV TYSDLLVVNK TDLAALVGAD
     LAVMARDADA VRDGRPTVLQ SLTEDPAASD VVAWVRSQLA ADGV