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UREE_YEREN
ID   UREE_YEREN              Reviewed;         230 AA.
AC   P42869;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Urease accessory protein UreE {ECO:0000255|HAMAP-Rule:MF_00822};
GN   Name=ureE {ECO:0000255|HAMAP-Rule:MF_00822};
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A2635 / Serotype O:8;
RX   PubMed=8045421; DOI=10.1016/0378-1119(94)90318-2;
RA   de Koning-Ward T.F., Ward A.C., Robins-Browne R.M.;
RT   "Characterisation of the urease-encoding gene complex of Yersinia
RT   enterocolitica.";
RL   Gene 145:25-32(1994).
RN   [2]
RP   ROLE IN VIRULENCE.
RC   STRAIN=W22703 / Serogroup O:9;
RX   PubMed=7558281; DOI=10.1128/iai.63.10.3790-3795.1995;
RA   de Koning-Ward T.F., Robins-Browne R.M.;
RT   "Contribution of urease to acid tolerance in Yersinia enterocolitica.";
RL   Infect. Immun. 63:3790-3795(1995).
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   -!- FUNCTION: Expression of the urease operon increases the likelihood of
CC       bacterial survival by contibuting to acid resistance in vitro and in
CC       vivo in BALB/c mice. Y.enterocolitica enters the body via an oral path
CC       and must survive the acidic stomach before being able to colonize the
CC       intestinal mucosa (PubMed:7558281). {ECO:0000269|PubMed:7558281}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00822}.
CC   -!- SIMILARITY: Belongs to the UreE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00822}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA50997.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L24101; AAA50997.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005172973.1; NZ_NWMR01000089.1.
DR   AlphaFoldDB; P42869; -.
DR   SMR; P42869; -.
DR   OrthoDB; 1663151at2; -.
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   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Nickel; Nickel insertion; Virulence.
FT   CHAIN           1..230
FT                   /note="Urease accessory protein UreE"
FT                   /id="PRO_0000067640"
FT   REGION          200..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  25746 MW;  6A0BAD7C30620F67 CRC64;
     MILIEHILGN VKKDPVWQEK LKDATFDLLV LDQREAQKSR CRKLSTQGLD LGISLDRHVV
     LADGDVLAWD EKTNVAVVVQ INLRDVMVID LSELKSRSPD ELIKTCFELG HALGNQHWKA
     VTKNNEVYVP LTVATTMMDS VMRTHGFQHL PFRFVKGAEI LPLLSNSEAR LLFGGAEDTD
     THVHVASPLD EPHGSGLHVH AIHSHGTGHT HSHDHDHSHS HGDHDHDHKH
 
 
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