UREE_BIFLS
ID UREE_BIFLS Reviewed; 221 AA.
AC B7GT18; E8MMX0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Urease accessory protein UreE {ECO:0000255|HAMAP-Rule:MF_00822};
GN Name=ureE {ECO:0000255|HAMAP-Rule:MF_00822};
GN OrderedLocusNames=Blon_0112, BLIJ_0113;
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAJ67708.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001095; ACJ51241.1; -; Genomic_DNA.
DR EMBL; AP010889; BAJ67708.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012576562.1; NZ_JDTT01000004.1.
DR AlphaFoldDB; B7GT18; -.
DR SMR; B7GT18; -.
DR PRIDE; B7GT18; -.
DR EnsemblBacteria; ACJ51241; ACJ51241; Blon_0112.
DR KEGG; bln:Blon_0112; -.
DR KEGG; blon:BLIJ_0113; -.
DR PATRIC; fig|391904.8.peg.117; -.
DR HOGENOM; CLU_1248634_0_0_11; -.
DR Proteomes; UP000001360; Chromosome.
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 HAMAP; MF_00822; UreE; 1.
DR InterPro; IPR012406; UreE.
DR InterPro; IPR007864; UreE_C_dom.
DR Pfam; PF05194; UreE_C; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Nickel.
FT CHAIN 1..221
FT /note="Urease accessory protein UreE"
FT /id="PRO_1000148715"
FT REGION 160..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 24703 MW; 410C39DEC3E1A0A0 CRC64;
MQTKGGSRLM IANRISGNII SDTFSDGKLN VPIEFEWFEA DKKRMRKVAA DGTEFGVAVG
ATIADGDVLA ETADKRYFAR IRTAQLIEIP VHSMKEMGRL CFELGNRHLS LKVEDDRVLV
PYDHPTMEYT KKIGFDPRVI EGGFDGFLIV KAHAGAGTIV PGTNKTTGDL AEEEQETERH
EPHAHAIGEH HHEKSEYEVN GVLHRADGMH SHDHGQTWHM H
