URED_SPOPA
ID URED_SPOPA Reviewed; 257 AA.
AC Q45347; Q93KP8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Urease accessory protein UreD {ECO:0000255|HAMAP-Rule:MF_01384};
GN Name=ureD {ECO:0000255|HAMAP-Rule:MF_01384};
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;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-207.
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).
CC -!- FUNCTION: Required for maturation of urease via the functional
CC incorporation of the urease nickel metallocenter. {ECO:0000255|HAMAP-
CC Rule:MF_01384}.
CC -!- SUBUNIT: UreD, UreF and UreG form a complex that acts as a GTP-
CC hydrolysis-dependent molecular chaperone, activating the urease
CC apoprotein by helping to assemble the nickel containing metallocenter
CC of UreC. The UreE protein probably delivers the nickel.
CC {ECO:0000255|HAMAP-Rule:MF_01384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01384}.
CC -!- SIMILARITY: Belongs to the UreD family. {ECO:0000255|HAMAP-
CC Rule:MF_01384}.
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DR EMBL; AF361945; AAK43720.1; -; Genomic_DNA.
DR EMBL; U29368; AAA73990.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45347; -.
DR SMR; Q45347; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR HAMAP; MF_01384; UreD; 1.
DR InterPro; IPR002669; UreD.
DR PANTHER; PTHR33643; PTHR33643; 1.
DR Pfam; PF01774; UreD; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Nickel insertion.
FT CHAIN 1..257
FT /note="Urease accessory protein UreD"
FT /id="PRO_0000067605"
FT CONFLICT 192..195
FT /note="MWFV -> WVD (in Ref. 2; AAA73990)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="E -> G (in Ref. 2; AAA73990)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..207
FT /note="DIREL -> RILGS (in Ref. 2; AAA73990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 29291 MW; 5889FD6328420B45 CRC64;
MEFQYRGNKT VLSNCYQNPP LRASRPLYIN PANRSEATVY LVETSGGIVE GDHNVFDIDI
KEGADVCLIP QSATKIYPSY NGIWSSQDMD ITIGPKASLS FKTEAVIPFE QARFNSKTVI
QMTSDSTFLW GDILSPGRVA RGEVFEYTDV RTNFQVWMDD ECLIYDPLLI SKDNMGLKKM
GMLEDHLFIG SMWFVTPTIE EFDIRELNER LQESPHSKAS ASMLEGKAVN VRWLASDLVD
LKKEMNRIWD EFANYIV