UREG2_BRUSU
ID UREG2_BRUSU Reviewed; 212 AA.
AC Q8FZV9; G0KB46;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Urease accessory protein UreG 2 {ECO:0000255|HAMAP-Rule:MF_01389};
GN Name=ureG2 {ECO:0000255|HAMAP-Rule:MF_01389}; Synonyms=ureG-2;
GN OrderedLocusNames=BR1361, BS1330_I1356;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP OPERON DISRUPTION, AND LACK OF ROLE IN VIRULENCE.
RC STRAIN=1330;
RX PubMed=17578575; DOI=10.1186/1471-2180-7-57;
RA Bandara A.B., Contreras A., Contreras-Rodriguez A., Martins A.M.,
RA Dobrean V., Poff-Reichow S., Rajasekaran P., Sriranganathan N.,
RA Schurig G.G., Boyle S.M.;
RT "Brucella suis urease encoded by ure1 but not ure2 is necessary for
RT intestinal infection of BALB/c mice.";
RL BMC Microbiol. 7:57-57(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 -!- FUNCTION: Disrupting the ure2 operon has no effect on urease activity,
CC or pathogen survival in BALB/c mice when inoculated by gavage, but
CC confers slightly enhanced resistance to low pH killing in vitro.
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; AE014291; AAN30275.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18692.1; -; Genomic_DNA.
DR RefSeq; WP_006190569.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8FZV9; -.
DR SMR; Q8FZV9; -.
DR EnsemblBacteria; AEM18692; AEM18692; BS1330_I1356.
DR GeneID; 45052381; -.
DR KEGG; bms:BR1361; -.
DR KEGG; bsi:BS1330_I1356; -.
DR PATRIC; fig|204722.21.peg.836; -.
DR HOGENOM; CLU_072144_1_0_5; -.
DR OMA; TQEDAQH; -.
DR PhylomeDB; Q8FZV9; -.
DR Proteomes; UP000007104; Chromosome I.
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.
FT CHAIN 1..212
FT /note="Urease accessory protein UreG 2"
FT /id="PRO_0000347364"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ SEQUENCE 212 AA; 22954 MW; E9359A82F8FAF123 CRC64;
MKKIPRIGVG GPVGSGKMAI IEAVVPILIK LGYRILVITN DIVTTEDAKH VQRTLKGVLI
EDRIVGVETG GCPHTAVRED PSMNLAAVEE MEAKFPDTDL VLLESGGDNL TLTFSPALID
FFIYVIDVAA GDKIPCKNGP GISQSDILVI NKTDLAPYVG ASLQVMDDDS RMMRGKKPFV
FTNCKTNEGI DDLVHLIREN VLFDTEVSKE SA
