ID   UREE1_BRUA2             Reviewed;         171 AA.
AC   P0C145; Q2YPD4; Q57F84; Q93T80;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Urease accessory protein UreE 1 {ECO:0000255|HAMAP-Rule:MF_00822};
GN   Name=ureE1 {ECO:0000255|HAMAP-Rule:MF_00822}; OrderedLocusNames=BAB1_0301;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF ROLE IN
RP   VIRULENCE.
RX   PubMed=17101645; DOI=10.1128/iai.01244-06;
RA   Sangari F.J., Seoane A., Rodriguez M.C., Aguero J., Garcia Lobo J.M.;
RT   "Characterization of the urease operon of Brucella abortus and assessment
RT   of its role in virulence of the bacterium.";
RL   Infect. Immun. 75:774-780(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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   -!- FUNCTION: Disruption of the ure1 gene cluster suggests that it protects
CC       brucellae during their passage through the stomach. The major route of
CC       infection in human brucellosis is oral.
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; AF361941; AAK51070.1; -; Genomic_DNA.
DR   EMBL; AM040264; CAJ10257.1; -; Genomic_DNA.
DR   PIR; AE3458; AE3458.
DR   RefSeq; WP_002963435.1; NZ_KN046823.1.
DR   AlphaFoldDB; P0C145; -.
DR   SMR; P0C145; -.
DR   STRING; 359391.BAB1_0301; -.
DR   EnsemblBacteria; CAJ10257; CAJ10257; BAB1_0301.
DR   GeneID; 3787079; -.
DR   KEGG; bmf:BAB1_0301; -.
DR   PATRIC; fig|359391.11.peg.2349; -.
DR   HOGENOM; CLU_093757_1_0_5; -.
DR   OMA; AYDARCK; -.
DR   PhylomeDB; P0C145; -.
DR   Proteomes; UP000002719; 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   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Nickel; Nickel insertion; Reference proteome;
KW   Virulence.
FT   CHAIN           1..171
FT                   /note="Urease accessory protein UreE 1"
FT                   /id="PRO_0000223405"
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