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Database: UniProt
Entry: V6JIK3_STRNV
LinkDB: V6JIK3_STRNV
Original site: V6JIK3_STRNV 
ID   V6JIK3_STRNV            Unreviewed;       231 AA.
AC   V6JIK3;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Urease accessory protein UreG {ECO:0000256|HAMAP-Rule:MF_01389};
GN   Name=ureG {ECO:0000256|HAMAP-Rule:MF_01389};
GN   ORFNames=M877_35935 {ECO:0000313|EMBL:EST19558.1};
OS   Streptomyces niveus NCIMB 11891.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST19558.1, ECO:0000313|Proteomes:UP000017971};
RN   [1] {ECO:0000313|EMBL:EST19558.1, ECO:0000313|Proteomes:UP000017971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST19558.1,
RC   ECO:0000313|Proteomes:UP000017971};
RX   PubMed=24407644;
RA   Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT   Aminocoumarin Antibiotic Novobiocin.";
RL   Genome Announc. 2:e01146-e01113(2014).
CC   -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC       metallocenter. This process requires GTP hydrolysis, probably
CC       effectuated by UreG. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01389}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01389}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC       subfamily. {ECO:0000256|ARBA:ARBA00005732, ECO:0000256|HAMAP-
CC       Rule:MF_01389}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EST19558.1}.
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DR   EMBL; AWQW01000290; EST19558.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6JIK3; -.
DR   STRING; 193462.BBN63_30575; -.
DR   PATRIC; fig|1352941.4.peg.7280; -.
DR   eggNOG; COG0378; Bacteria.
DR   HOGENOM; CLU_072144_1_0_11; -.
DR   Proteomes; UP000017971; 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   CDD; cd05540; UreG; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00101; ureG; 1.
DR   PANTHER; PTHR31715; UREASE ACCESSORY PROTEIN G; 1.
DR   PANTHER; PTHR31715:SF0; UREASE ACCESSORY PROTEIN G; 1.
DR   Pfam; PF02492; cobW; 1.
DR   PIRSF; PIRSF005624; Ni-bind_GTPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01389};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01389};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01389};
KW   Nickel insertion {ECO:0000256|ARBA:ARBA00022988, ECO:0000256|HAMAP-
KW   Rule:MF_01389};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01389}.
FT   DOMAIN          35..205
FT                   /note="CobW/HypB/UreG nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02492"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39..46
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01389"
SQ   SEQUENCE   231 AA;  24379 MW;  13456C354ED899F7 CRC64;
     MHLDHADPYT DPYLDPHHHG AGATRPDGSR RALRIGLGGP VGSGKTATVA ALCRALRDQW
     SIAVVTNDIY TREDAAFLLR NAVLPAERIQ AVETGACPHT AIRDDISANL EAVEDLEDSV
     GPLDLILVES GGDNLTATFS KGLVDAQIFV IDVAGGDDIP RKGGPGVTTS DLLVINKTDL
     APYVGSDLGR MASDAKEQRG ELPVLFTSLT GPDGVAPVAD WVRARRAAWI A
//
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