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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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