ID   UREG1_SACEN             Reviewed;         248 AA.
AC   A4F7F9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Urease accessory protein UreG 1 {ECO:0000255|HAMAP-Rule:MF_01389};
GN   Name=ureG1 {ECO:0000255|HAMAP-Rule:MF_01389}; OrderedLocusNames=SACE_0638;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAL99983.1; -; Genomic_DNA.
DR   RefSeq; WP_009950038.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4F7F9; -.
DR   SMR; A4F7F9; -.
DR   STRING; 405948.SACE_0638; -.
DR   EnsemblBacteria; CAL99983; CAL99983; SACE_0638.
DR   KEGG; sen:SACE_0638; -.
DR   eggNOG; COG0378; Bacteria.
DR   HOGENOM; CLU_072144_1_0_11; -.
DR   OMA; PHFHADE; -.
DR   OrthoDB; 1134430at2; -.
DR   Proteomes; UP000006728; 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; GTP-binding; Nickel insertion; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..248
FT                   /note="Urease accessory protein UreG 1"
FT                   /id="PRO_0000347445"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53..60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   248 AA;  25950 MW;  1F50B404FD67638D CRC64;
     MLPEHHDHGH EHGGNGHGHG HRHQVNFDPT AAEPDPYGVA PRGGRAFRLG IGGPVGSGKT
     ALTAALCRAL GSEVNLAVVT NDIYTTEDAD FLRRAGVLDT DRIEAVQTGA CPHTAIRDDI
     TANLDAVEKL EERHPGLELV IVESGGDNLT AVFSRGLADS QVFVVDVAGG DKVPRKGGPG
     VTTADLLVIN KVDLAEQVGA DMAVMVADAH RMRGELPVIT QSLTRTPNAP DVSAWVRQQL
     AAGVVVGA