UREG_ANADF
ID UREG_ANADF Reviewed; 236 AA.
AC A7HHN3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389};
GN Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389};
GN OrderedLocusNames=Anae109_4051;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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; CP000769; ABS28229.1; -; Genomic_DNA.
DR RefSeq; WP_012098867.1; NC_009675.1.
DR AlphaFoldDB; A7HHN3; -.
DR SMR; A7HHN3; -.
DR STRING; 404589.Anae109_4051; -.
DR EnsemblBacteria; ABS28229; ABS28229; Anae109_4051.
DR KEGG; afw:Anae109_4051; -.
DR eggNOG; COG0378; Bacteria.
DR HOGENOM; CLU_072144_0_0_7; -.
DR OMA; VDLTIYV; -.
DR OrthoDB; 1134430at2; -.
DR Proteomes; UP000006382; 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 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 Reference proteome.
FT CHAIN 1..236
FT /note="Urease accessory protein UreG"
FT /id="PRO_0000347345"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01389"
SQ SEQUENCE 236 AA; 24970 MW; BF81C8B78ED0D5E5 CRC64;
MHDHSLHSGH DHGLGPGSFH DRGAPHARGD LRRRAFTVGV GGPVGSGKTA LVLALCRALR
DSRSLGVVTN DIFTREDAEF LVRNDALPAE RIRAVETGGC PHAAIREDVT ANLLALEELT
EAHRPEILFC ESGGDNLAAH FSRELADYTI YVIDVAGGDK VPRKGGPGIT QADLLVVNKT
DLATAVGADL DVMARDAARM RGDGPVVFAQ VTRGVGVPEI AGHVLHAYRH AVGAPH