ID   URED_KLEAE              Reviewed;         270 AA.
AC   Q09063;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Urease accessory protein UreD {ECO:0000255|HAMAP-Rule:MF_01384};
GN   Name=ureD {ECO:0000255|HAMAP-Rule:MF_01384};
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].
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   [2]
RP   INTERACTION WITH UREASE APOPROTEIN, AND POSSIBLE CHAPERONE ACTIVITY IN
RP   NICKEL METALLOCENTER ASSEMBLY.
RX   PubMed=7909161; DOI=10.1073/pnas.91.8.3233;
RA   Park I.-S., Carr M.B., Hausinger R.P.;
RT   "In vitro activation of urease apoprotein and role of UreD as a chaperone
RT   required for nickel metallocenter assembly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3233-3237(1994).
RN   [3]
RP   CATALYTIC ACTIVITY, AND INTERACTION WITH UREA; UREB; UREC; UREF AND UREG.
RX   PubMed=7721685; DOI=10.1128/jb.177.8.1947-1951.1995;
RA   Park I.-S., Hausinger R.P.;
RT   "Evidence for the presence of urease apoprotein complexes containing UreD,
RT   UreF, and UreG in cells that are competent for in vivo enzyme activation.";
RL   J. Bacteriol. 177:1947-1951(1995).
RN   [4]
RP   COMPLEX FORMATION, AND INTERACTION WITH UREA; UREB; UREC; UREF AND UREG.
RX   PubMed=10500143; DOI=10.1073/pnas.96.20.11140;
RA   Soriano A., Hausinger R.P.;
RT   "GTP-dependent activation of urease apoprotein in complex with the UreD,
RT   UreF, and UreG accessory proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999).
RN   [5]
RP   INTERACTION WITH UREB AND UREC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14749331; DOI=10.1074/jbc.m312979200;
RA   Chang Z., Kuchar J., Hausinger R.P.;
RT   "Chemical cross-linking and mass spectrometric identification of sites of
RT   interaction for UreD, UreF, and urease.";
RL   J. Biol. Chem. 279:15305-15313(2004).
CC   -!- FUNCTION: Necessary for the functional incorporation of the urease
CC       nickel metallocenter.
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 complex may form in the order UreABCD, UreABCDF,
CC       UreABCDFG. The UreE protein probably delivers the nickel in a GTPase-
CC       dependent fashion.
CC   -!- INTERACTION:
CC       Q09063; P18318: ureF; NbExp=4; IntAct=EBI-6410589, EBI-6410604;
CC       Q09063; P18319: ureG; NbExp=4; IntAct=EBI-6410589, EBI-6410613;
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; M55391; AAA25148.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q09063; -.
DR   SMR; Q09063; -.
DR   IntAct; Q09063; 6.
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   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Nickel insertion.
FT   CHAIN           1..270
FT                   /note="Urease accessory protein UreD"
FT                   /id="PRO_0000067611"
SQ   SEQUENCE   270 AA;  29840 MW;  F87D0647DFB7FE91 CRC64;
     MLPPLKKGWQ ATLDLRFHQA GGKTVLASAQ HVGPLTVQRP FYPEEETCHL YLLHPPGGIV
     GGDELTISAH LAPGCHTLIT MPGASKFYRS SGAQALVRQQ LTLAPQATLE WLPQDAIFFP
     GANARLFTTF HLCASSRLLA WDLLCLGRPV IGETFSHGTL SNRLEVWVDN EPLLVERLHL
     QEGELSSIAE RPWVGTLLCY PATDALLDGV RDALAPLGLY AGASLTDRLL TVRFLSDDNL
     ICQRVMRDVW QFLRPHLTGK SPVLPRIWLT