ID   UREE_BRASO              Reviewed;         210 AA.
AC   A4YM31;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Urease accessory protein UreE {ECO:0000255|HAMAP-Rule:MF_00822};
GN   Name=ureE {ECO:0000255|HAMAP-Rule:MF_00822}; OrderedLocusNames=BRADO1043;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
CC   -!- FUNCTION: Involved in urease metallocenter assembly. Binds nickel.
CC       Probably functions as a nickel donor during metallocenter assembly.
CC       {ECO:0000255|HAMAP-Rule:MF_00822}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00822}.
CC   -!- SIMILARITY: Belongs to the UreE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00822}.
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DR   EMBL; CU234118; CAL74957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YM31; -.
DR   SMR; A4YM31; -.
DR   STRING; 114615.BRADO1043; -.
DR   EnsemblBacteria; CAL74957; CAL74957; BRADO1043.
DR   KEGG; bra:BRADO1043; -.
DR   eggNOG; COG2371; Bacteria.
DR   HOGENOM; CLU_093757_1_0_5; -.
DR   OMA; AYDARCK; -.
DR   BioCyc; BSP114615:BRADO_RS33715-MON; -.
DR   Proteomes; UP000001994; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:InterPro.
DR   GO; GO:0019627; P:urea metabolic process; IEA:InterPro.
DR   CDD; cd00571; UreE; 1.
DR   HAMAP; MF_00822; UreE; 1.
DR   InterPro; IPR012406; UreE.
DR   InterPro; IPR007864; UreE_C_dom.
DR   InterPro; IPR004029; UreE_N.
DR   InterPro; IPR036118; UreE_N_sf.
DR   Pfam; PF05194; UreE_C; 1.
DR   Pfam; PF02814; UreE_N; 1.
DR   SMART; SM00988; UreE_N; 1.
DR   SUPFAM; SSF69287; SSF69287; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Nickel; Nickel insertion; Reference proteome.
FT   CHAIN           1..210
FT                   /note="Urease accessory protein UreE"
FT                   /id="PRO_1000062543"
FT   REGION          136..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  23714 MW;  F840DE1B530D8386 CRC64;
     MIRATRVLGQ HRWKEAAADS VLLDFDDRHR RRLAMTGTRG LEFLLDLEHA TALRGGDALV
     LEDGRLIEVV AAAEPLLEIR AGDPHHLVRL AWHLGNRHLP TQIMAKSLRI RRDHVIEAMV
     KGLGARVIEI EAPFDPEGGA YAEPSHAHGD HDHDHHGHDH HGHDHTSHDH AHHSHAHHDH
     DHGHAHDDHV HDEHCGHDHH HGHSHAHDHK