UREG_ARATH
ID UREG_ARATH Reviewed; 275 AA.
AC O64700; Q9SYT8;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Urease accessory protein G;
DE Short=AtUREG;
GN Name=UREG; OrderedLocusNames=At2g34470;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Freyermuth S.K., Forde B.G., Polacco J.C.;
RT "Nucleotide sequence of a cDNA encoding an Arabidopsis urease accessory
RT protein.";
RL (er) Plant Gene Register PGR99-012(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16244137; DOI=10.1104/pp.105.070292;
RA Witte C.P., Rosso M.G., Romeis T.;
RT "Identification of three urease accessory proteins that are required for
RT urease activation in Arabidopsis.";
RL Plant Physiol. 139:1155-1162(2005).
CC -!- FUNCTION: Required for the maturation and activation of urease via the
CC functional incorporation of the urease nickel metallocenter.
CC {ECO:0000269|PubMed:16244137}.
CC -!- SUBUNIT: URED, UREF and UREG may form a complex that acts as a GTP-
CC hydrolysis-dependent molecular chaperone, activating the urease
CC apoprotein. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O64700-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants cannot grow on medium with urea as the
CC sole source of nitrogen. {ECO:0000269|PubMed:16244137}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC subfamily. {ECO:0000305}.
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DR EMBL; AF109374; AAD16984.1; -; mRNA.
DR EMBL; AC004077; AAC26700.1; -; Genomic_DNA.
DR EMBL; AC004481; AAM14950.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08978.1; -; Genomic_DNA.
DR EMBL; AK119138; BAC43708.1; -; mRNA.
DR EMBL; BT005276; AAO63340.1; -; mRNA.
DR EMBL; AY085812; AAM63028.1; -; mRNA.
DR PIR; T02334; T02334.
DR PIR; T52333; T52333.
DR RefSeq; NP_180994.1; NM_128999.3. [O64700-1]
DR AlphaFoldDB; O64700; -.
DR SMR; O64700; -.
DR BioGRID; 3357; 2.
DR ComplexPortal; CPX-1296; Urease activation complex.
DR STRING; 3702.AT2G34470.2; -.
DR iPTMnet; O64700; -.
DR PaxDb; O64700; -.
DR PRIDE; O64700; -.
DR ProMEX; O64700; -.
DR ProteomicsDB; 228630; -. [O64700-1]
DR EnsemblPlants; AT2G34470.1; AT2G34470.1; AT2G34470. [O64700-1]
DR GeneID; 818010; -.
DR Gramene; AT2G34470.1; AT2G34470.1; AT2G34470. [O64700-1]
DR KEGG; ath:AT2G34470; -.
DR Araport; AT2G34470; -.
DR eggNOG; ENOG502QR6E; Eukaryota.
DR OMA; VDLTIYV; -.
DR PhylomeDB; O64700; -.
DR PRO; PR:O64700; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64700; baseline and differential.
DR Genevisible; O64700; AT.
DR GO; GO:0150006; C:urease activator complex; IPI:ComplexPortal.
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:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:UniProtKB.
DR GO; GO:0043419; P:urea catabolic process; IDA:ComplexPortal.
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 2: Evidence at transcript level;
KW Alternative splicing; Chaperone; GTP-binding; Nickel insertion;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..275
FT /note="Urease accessory protein G"
FT /id="PRO_0000424255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 7
FT /note="H -> P (in Ref. 1; AAD16984)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="L -> P (in Ref. 1; AAD16984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 30083 MW; 1D054F4E0C3CE7D7 CRC64;
MASHDHHHHH HDHEHDHEKS DGGEGKASWV GKDGKVYHSH DGLAPHSHEP IYSPGYFSRR
APPLHDRNFS ERAFTVGIGG PVGTGKTALM LALCRFLRDK YSLAAVTNDI FTKEDGEFLV
KNGALPEERI RAVETGGCPH AAIREDISIN LGPLEELSNL FKADLLLCES GGDNLAANFS
RELADYIIYI IDVSAGDKIP RKGGPGITQA DLLVINKTDL AAAVGADLSV MERDSLRMRD
GGPFVFAQVK HGLGVEEIVN HVMHSWEHAT GKKRQ