ID C5S4A1_9PAST Unreviewed; 211 AA.
AC C5S4A1;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Urease accessory protein UreG {ECO:0000256|HAMAP-Rule:MF_01389};
GN Name=ureG {ECO:0000256|HAMAP-Rule:MF_01389};
GN ORFNames=AM305_02433 {ECO:0000313|EMBL:EER46271.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER46271.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER46271.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER46271.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
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:EER46271.1}.
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DR EMBL; ACQL01000131; EER46271.1; -; Genomic_DNA.
DR RefSeq; WP_005825593.1; NZ_ACQL01000131.1.
DR AlphaFoldDB; C5S4A1; -.
DR eggNOG; COG0378; Bacteria.
DR OrthoDB; 9802035at2; -.
DR Proteomes; UP000005532; Unassembled WGS sequence.
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 7..177
FT /note="CobW/HypB/UreG nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF02492"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01389"
SQ SEQUENCE 211 AA; 23114 MW; DA1B1F4A75034E8C CRC64;
MRKYIKIGVA GPVGAGKTAL IEKLTREIAS KYSVAVITND IYTQEDAEFL TKNSLLPPER
IMGVETGGCP HTAIREDASM NLEAVDEMVA RFPDVEIVFI ESGGDNLSAT FSPDLADVTI
FVIDVAQGEK IPRKGGPGIT RSDLLVINKT DLAPFVGADL SVMERDARRM RNGQPFIFTN
LMKKENLDGV IGWIEKYALL KNVEEPSSLV R
//
