UREG1_BRUME
ID UREG1_BRUME Reviewed; 208 AA.
AC Q7CNT4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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}; OrderedLocusNames=BMEI1649;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL52830.1; -; Genomic_DNA.
DR RefSeq; WP_002963437.1; NZ_GG703778.1.
DR AlphaFoldDB; Q7CNT4; -.
DR SMR; Q7CNT4; -.
DR STRING; 224914.BMEI1649; -.
DR EnsemblBacteria; AAL52830; AAL52830; BMEI1649.
DR GeneID; 45051406; -.
DR GeneID; 55590052; -.
DR KEGG; bme:BMEI1649; -.
DR PATRIC; fig|224914.52.peg.1942; -.
DR eggNOG; COG0378; Bacteria.
DR OMA; VDLTIYV; -.
DR PhylomeDB; Q7CNT4; -.
DR Proteomes; UP000000419; 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..208
FT /note="Urease accessory protein UreG 1"
FT /id="PRO_0000347360"
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
