ID   UREE_RHIL3              Reviewed;         198 AA.
AC   Q1MCW2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Urease accessory protein UreE {ECO:0000255|HAMAP-Rule:MF_00822};
GN   Name=ureE {ECO:0000255|HAMAP-Rule:MF_00822}; OrderedLocusNames=RL3728;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(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; AM236080; CAK09218.1; -; Genomic_DNA.
DR   RefSeq; WP_011653182.1; NC_008380.1.
DR   AlphaFoldDB; Q1MCW2; -.
DR   SMR; Q1MCW2; -.
DR   STRING; 216596.RL3728; -.
DR   EnsemblBacteria; CAK09218; CAK09218; RL3728.
DR   KEGG; rle:RL3728; -.
DR   eggNOG; COG2371; Bacteria.
DR   HOGENOM; CLU_093757_1_0_5; -.
DR   OMA; AYDARCK; -.
DR   Proteomes; UP000006575; 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.
FT   CHAIN           1..198
FT                   /note="Urease accessory protein UreE"
FT                   /id="PRO_1000213118"
FT   REGION          137..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..198
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  22814 MW;  10E2425E337C4109 CRC64;
     MQRVTSYLPA GTPSSHPIAQ VKLPHDLRHL RRKLLHLENG EMVMLDLKDP VLFANGDLLV
     RDDGELIEIL AADEKLFEIR GRDRTHLVEL AWHLGNRHLA AQIEEDRIVI LRDHVIRAML
     QGLGAVVLEI DEPFQPARGA YHSPGGHSHG HDHDHNHDHG HDHAHDHNHG HDHDHEHGYE
     HEHEHRHDRG HDHDHKHD