UREE_PARXL
ID UREE_PARXL Reviewed; 225 AA.
AC Q144E5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Urease accessory protein UreE {ECO:0000255|HAMAP-Rule:MF_00822};
GN Name=ureE {ECO:0000255|HAMAP-Rule:MF_00822}; OrderedLocusNames=Bxeno_A0756;
GN ORFNames=Bxe_A3695;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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 -!- 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; CP000270; ABE29294.1; -; Genomic_DNA.
DR RefSeq; WP_011487080.1; NZ_CP008760.1.
DR AlphaFoldDB; Q144E5; -.
DR SMR; Q144E5; -.
DR STRING; 266265.Bxe_A3695; -.
DR EnsemblBacteria; ABE29294; ABE29294; Bxe_A3695.
DR KEGG; bxb:DR64_1387; -.
DR KEGG; bxe:Bxe_A3695; -.
DR PATRIC; fig|266265.5.peg.776; -.
DR eggNOG; COG2371; Bacteria.
DR OMA; AYDARCK; -.
DR OrthoDB; 1663151at2; -.
DR Proteomes; UP000001817; Chromosome 1.
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 SMART; SM00988; UreE_N; 1.
DR SUPFAM; SSF69287; SSF69287; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Nickel; Nickel insertion; Reference proteome.
FT CHAIN 1..225
FT /note="Urease accessory protein UreE"
FT /id="PRO_1000083886"
FT REGION 171..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 225 AA; 24768 MW; C839DD9AE24680F5 CRC64;
MRTIDKLIAP HLKLAPVLVK RAPTLTLAFD DRRKSRLAAT LDSGEEVALL LPRGTVLRDG
DVLVADDGGL VRVIAAPEAV LYVRAKDALT LTRAAYHLGN RHTPVEVGAD YLKLEFDPVL
ADMLKRIGAT VDQVSMPFQP ESGAYGGGHK HGHDETFAED YALAQQVFGE HHGHEHSHDH
EHGHSHAAHE HSHGHDHTHG HDHDHGDHVH DESCGHGHHH HHAHR