ID   UREE_BRUME              Reviewed;         171 AA.
AC   Q7CNT3;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Urease accessory protein UreE {ECO:0000255|HAMAP-Rule:MF_00822};
GN   Name=ureE {ECO:0000255|HAMAP-Rule:MF_00822}; OrderedLocusNames=BMEI1651;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL52832.1; -; Genomic_DNA.
DR   RefSeq; WP_002963435.1; NC_003317.1.
DR   AlphaFoldDB; Q7CNT3; -.
DR   SMR; Q7CNT3; -.
DR   STRING; 224914.BMEI1651; -.
DR   EnsemblBacteria; AAL52832; AAL52832; BMEI1651.
DR   GeneID; 3787079; -.
DR   KEGG; bme:BMEI1651; -.
DR   eggNOG; COG2371; Bacteria.
DR   OMA; AYDARCK; -.
DR   PhylomeDB; Q7CNT3; -.
DR   Proteomes; UP000000419; Chromosome I.
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..171
FT                   /note="Urease accessory protein UreE"
FT                   /id="PRO_0000223406"
FT   REGION          143..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   171 AA;  19492 MW;  BE6064EE8CF2D21E CRC64;
     MFRAIAIIRA HEVIDAVPAS HIVLERDERH LRRKAITLEN GEKILADFAE PVVLEHGDRL
     VLDDGREIEI RAASEELYEI RGRDPRHIAE LAWHIGNRHL AAQIETDHIF ILRDHVIRVM
     LEGLGATVTD VVAIFSPLRG AYSGGHQHHH GHDHDHGHHG HDHDHHHPDH E