ID   UREE_YERE8              Reviewed;         230 AA.
AC   A1JKE0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Urease accessory protein UreE {ECO:0000255|HAMAP-Rule:MF_00822};
GN   Name=ureE {ECO:0000255|HAMAP-Rule:MF_00822}; OrderedLocusNames=YE0954;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL11052.1; -; Genomic_DNA.
DR   RefSeq; WP_005172973.1; NC_008800.1.
DR   RefSeq; YP_001005288.1; NC_008800.1.
DR   AlphaFoldDB; A1JKE0; -.
DR   SMR; A1JKE0; -.
DR   STRING; 393305.YE0954; -.
DR   EnsemblBacteria; CAL11052; CAL11052; YE0954.
DR   KEGG; yen:YE0954; -.
DR   PATRIC; fig|393305.7.peg.1055; -.
DR   eggNOG; COG2371; Bacteria.
DR   HOGENOM; CLU_095954_0_0_6; -.
DR   OMA; HAIGNQH; -.
DR   Proteomes; UP000000642; 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   PIRSF; PIRSF036402; Ureas_acces_UreE; 1.
DR   SMART; SM00988; UreE_N; 1.
DR   SUPFAM; SSF69287; SSF69287; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Nickel; Nickel insertion.
FT   CHAIN           1..230
FT                   /note="Urease accessory protein UreE"
FT                   /id="PRO_1000062566"
FT   REGION          200..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  25746 MW;  6A0BAD7C30620F67 CRC64;
     MILIEHILGN VKKDPVWQEK LKDATFDLLV LDQREAQKSR CRKLSTQGLD LGISLDRHVV
     LADGDVLAWD EKTNVAVVVQ INLRDVMVID LSELKSRSPD ELIKTCFELG HALGNQHWKA
     VTKNNEVYVP LTVATTMMDS VMRTHGFQHL PFRFVKGAEI LPLLSNSEAR LLFGGAEDTD
     THVHVASPLD EPHGSGLHVH AIHSHGTGHT HSHDHDHSHS HGDHDHDHKH