UREE_KLEAE
ID UREE_KLEAE Reviewed; 158 AA.
AC P18317;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Urease accessory protein UreE;
GN Name=ureE;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CG253;
RX PubMed=2211515; DOI=10.1128/jb.172.10.5837-5843.1990;
RA Mulrooney S.B., Hausinger R.P.;
RT "Sequence of the Klebsiella aerogenes urease genes and evidence for
RT accessory proteins facilitating nickel incorporation.";
RL J. Bacteriol. 172:5837-5843(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-5, AND DISRUPTION PHENOTYPE.
RX PubMed=1624427; DOI=10.1128/jb.174.13.4324-4330.1992;
RA Lee M.H., Mulrooney S.B., Renner M.J., Markowicz Y., Hausinger R.P.;
RT "Klebsiella aerogenes urease gene cluster: sequence of ureD and
RT demonstration that four accessory genes (ureD, ureE, ureF, and ureG) are
RT involved in nickel metallocenter biosynthesis.";
RL J. Bacteriol. 174:4324-4330(1992).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8318889; DOI=10.1002/pro.5560020617;
RA Lee M.H., Pankratz H.S., Wang S., Scott R.A., Finnegan M.G., Johnson M.K.,
RA Ippolito J.A., Christianson D.W., Hausinger R.P.;
RT "Purification and characterization of Klebsiella aerogenes UreE protein: a
RT nickel-binding protein that functions in urease metallocenter assembly.";
RL Protein Sci. 2:1042-1052(1993).
RN [4]
RP UREE-UREF FUSION PROTEIN.
RX PubMed=17041056; DOI=10.1128/jb.01265-06;
RA Kim J.K., Mulrooney S.B., Hausinger R.P.;
RT "The UreEF fusion protein provides a soluble and functional form of the
RT UreF urease accessory protein.";
RL J. Bacteriol. 188:8413-8420(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-143.
RX PubMed=11591723; DOI=10.1074/jbc.m108619200;
RA Song H.K., Mulrooney S.B., Huber R., Hausinger R.P.;
RT "Crystal structure of Klebsiella aerogenes UreE, a nickel-binding
RT metallochaperone for urease activation.";
RL J. Biol. Chem. 276:49359-49364(2001).
CC -!- FUNCTION: Involved in urease metallocenter assembly. Binds about 6
CC nickel ions per homodimer. Probably functions as a nickel donor during
CC metallocenter assembly. Its function can be bypassed in vitro in the
CC presence of high nickel concentrations.
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Note=Binds 2 Ni ions per subunit.;
CC -!- SUBUNIT: Homodimer. Dimerization is prevented in the UreEF fusion
CC protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Disrupting the ure1 operon causes loss of urease
CC activity. {ECO:0000269|PubMed:1624427}.
CC -!- MISCELLANEOUS: The artificial UreEF fusion protein binds nickel but is
CC not able to transfer it to the apoprotein, thus its function is
CC impaired. UreF function seems largely unaltered in the fusion.
CC -!- SIMILARITY: Belongs to the UreE family. {ECO:0000305}.
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DR EMBL; M36068; AAA25152.1; -; Genomic_DNA.
DR PDB; 1GMU; X-ray; 1.50 A; A/B/C/D=1-143.
DR PDB; 1GMV; X-ray; 2.80 A; A/B=1-143.
DR PDB; 1GMW; X-ray; 1.50 A; A/B/C/D=1-143.
DR PDBsum; 1GMU; -.
DR PDBsum; 1GMV; -.
DR PDBsum; 1GMW; -.
DR AlphaFoldDB; P18317; -.
DR SMR; P18317; -.
DR IntAct; P18317; 1.
DR EvolutionaryTrace; P18317; -.
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 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Nickel; Nickel insertion.
FT CHAIN 1..158
FT /note="Urease accessory protein UreE"
FT /id="PRO_0000067635"
FT BINDING 96
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 110
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:1GMU"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1GMV"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1GMW"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:1GMU"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1GMU"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:1GMU"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1GMU"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1GMU"
SQ SEQUENCE 158 AA; 17559 MW; E17492AAE002AD2C CRC64;
MLYLTQRLEI PAAATASVTL PIDVRVKSRV KVTLNDGRDA GLLLPRGLLL RGGDVLSNEE
GTEFVQVIAA DEEVSVVRCD DPFMLAKACY HLGNRHVPLQ IMPGELRYHH DHVLDDMLRQ
FGLTVTFGQL PFEPEAGAYA SESHGHHHAH HDHHAHSH
