UREG1_BRUSU
ID UREG1_BRUSU Reviewed; 208 AA.
AC Q8G2P5; G0KBX2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Urease accessory protein UreG 1 {ECO:0000255|HAMAP-Rule:MF_01389};
GN Name=ureG1 {ECO:0000255|HAMAP-Rule:MF_01389}; Synonyms=ureG-1;
GN OrderedLocusNames=BR0273, BS1330_I0274;
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 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 ure1 operon causes loss of urease activity,
CC decreased resistance to low pH killing in vitro and decreased pathogen
CC survival when inoculated in BALB/c mice by gavage.
CC {ECO:0000269|PubMed:17578575}.
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; AAN29222.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM17635.1; -; Genomic_DNA.
DR PIR; AC3458; AC3458.
DR RefSeq; WP_002963437.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G2P5; -.
DR SMR; Q8G2P5; -.
DR EnsemblBacteria; AEM17635; AEM17635; BS1330_I0274.
DR GeneID; 45051406; -.
DR GeneID; 55590052; -.
DR KEGG; bms:BR0273; -.
DR KEGG; bsi:BS1330_I0274; -.
DR PATRIC; fig|204722.21.peg.1756; -.
DR HOGENOM; CLU_072144_1_0_5; -.
DR OMA; VDLTIYV; -.
DR PhylomeDB; Q8G2P5; -.
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;
KW Virulence.
FT CHAIN 1..208
FT /note="Urease accessory protein UreG 1"
FT /id="PRO_0000347363"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ SEQUENCE 208 AA; 22705 MW; 39FF82812CA4FDE2 CRC64;
MTQKNGPLRV GIGGPVGSGK TTLTEKLCKA MRDKYSVAVI TNDIYTQEDA LILARRQALS
EDRIIGVETG GCPHTAIRED ASINLQAVVE MTRRFPDLDV VFIESGGDNL AATFSPDLAD
LTLYVISVCQ GEEIPRKGGP GITRSDFLVI NKSDLAPYVH VDLEVMEADA MRMRAKRPFG
FTDLHRGKGV QEIIDFIVEN GGLEPRSN