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UREE_SPOPA
ID   UREE_SPOPA              Reviewed;         147 AA.
AC   P50049; Q9RP20;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Urease accessory protein UreE;
GN   Name=ureE;
OS   Sporosarcina pasteurii (Bacillus pasteurii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RA   You J.-H., Kim J.-G., Song B.-H., Lee M.-H., Kim S.-D.;
RT   "Genetic organization and nucleotide sequence of the ure gene cluster in
RT   Bacillus pasteurii.";
RL   Mol. Cells 5:359-369(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], COFACTOR, SUBUNIT, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822;
RX   PubMed=12072968; DOI=10.1007/s00775-002-0341-7;
RA   Ciurli S., Safarov N., Miletti S., Dikiy A., Christensen S.K.,
RA   Kornetzky K., Bryant D.A., Vandenberghe I., Devreese B., Samyn B.,
RA   Remaut H., Van Beeumen J.;
RT   "Molecular characterization of Bacillus pasteurii UreE, a metal-binding
RT   chaperone for the assembly of the urease active site.";
RL   J. Biol. Inorg. Chem. 7:623-631(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=11602602; DOI=10.1074/jbc.m108304200;
RA   Remaut H., Safarov N., Ciurli S., Van Beeumen J.;
RT   "Structural basis for Ni(2+) transport and assembly of the urease active
RT   site by the metallochaperone UreE from Bacillus pasteurii.";
RL   J. Biol. Chem. 276:49365-49370(2001).
CC   -!- FUNCTION: Involved in urease metallocenter assembly. Binds nickel.
CC       Probably functions as a nickel donor during metallocenter assembly.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:12072968};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000269|PubMed:12072968};
CC       Note=Binds 1 Zn(2+) or 1 Ni(2+) ion per dimer or tetramer.
CC       {ECO:0000269|PubMed:12072968};
CC   -!- SUBUNIT: Homodimer in diluted solutions, homotetramer in concentrated
CC       solutions and when bound to Ni(2+) or Zn(2+). The homodimer is thought
CC       to be the active form. {ECO:0000269|PubMed:12072968}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UreE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA73987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U29368; AAA73987.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF361945; AAD55059.1; -; Genomic_DNA.
DR   PDB; 1EAR; X-ray; 1.70 A; A=3-147.
DR   PDB; 1EB0; X-ray; 1.85 A; A=3-147.
DR   PDB; 4L3K; X-ray; 1.88 A; A/B=1-147.
DR   PDBsum; 1EAR; -.
DR   PDBsum; 1EB0; -.
DR   PDBsum; 4L3K; -.
DR   AlphaFoldDB; P50049; -.
DR   BMRB; P50049; -.
DR   SMR; P50049; -.
DR   EvolutionaryTrace; P50049; -.
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; Metal-binding; Nickel;
KW   Nickel insertion; Zinc.
FT   CHAIN           1..147
FT                   /note="Urease accessory protein UreE"
FT                   /id="PRO_0000067629"
FT   BINDING         100
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          18..25
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   HELIX           27..31
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:4L3K"
FT   STRAND          59..63
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          65..73
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          76..82
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   HELIX           86..98
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   HELIX           116..125
FT                   /evidence="ECO:0007829|PDB:1EAR"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:1EAR"
SQ   SEQUENCE   147 AA;  17402 MW;  8E07578B67230DD3 CRC64;
     MLITKIVGHI DDYESSDKKV DWLEVEWEDL NKRILRKETE NGTDIAIKLE NSGTLRYGDV
     LYESDDTLIA IRTKLEKVYV IKPQTMQEMG KMAFEIGNRH TMCIIEDDEI LVRYDKTLEK
     LIDEVGVSYE QSERRFKEPF KYRGHQH
 
 
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