ID   UREF_PROMH              Reviewed;         222 AA.
AC   P17091; B4EXN7;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Urease accessory protein UreF {ECO:0000255|HAMAP-Rule:MF_01385};
GN   Name=ureF {ECO:0000255|HAMAP-Rule:MF_01385}; OrderedLocusNames=PMI3687;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2687233; DOI=10.1128/jb.171.12.6414-6422.1989;
RA   Jones B.D., Mobley H.L.T.;
RT   "Proteus mirabilis urease: nucleotide sequence determination and comparison
RT   with jack bean urease.";
RL   J. Bacteriol. 171:6414-6422(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
RN   [3]
RP   UREASE AS A VIRULENCE FACTOR.
RX   PubMed=2180821; DOI=10.1128/iai.58.4.1120-1123.1990;
RA   Jones B.D., Lockatell C.V., Johnson D.E., Warren J.W., Mobley H.L.T.;
RT   "Construction of a urease-negative mutant of Proteus mirabilis: analysis of
RT   virulence in a mouse model of ascending urinary tract infection.";
RL   Infect. Immun. 58:1120-1123(1990).
RN   [4]
RP   PROBABLE OPERON STRUCTURE, AND MUTAGENESIS OF ILE-183.
RX   PubMed=7559355; DOI=10.1128/jb.177.19.5653-5660.1995;
RA   Island M.D., Mobley H.L.T.;
RT   "Proteus mirabilis urease: operon fusion and linker insertion analysis of
RT   ure gene organization, regulation, and function.";
RL   J. Bacteriol. 177:5653-5660(1995).
CC   -!- FUNCTION: Required for maturation of urease via the functional
CC       incorporation of the urease nickel metallocenter. {ECO:0000255|HAMAP-
CC       Rule:MF_01385}.
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 UreE protein probably delivers the nickel.
CC       {ECO:0000255|HAMAP-Rule:MF_01385}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01385}.
CC   -!- SIMILARITY: Belongs to the UreF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01385}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25671.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M31834; AAA25671.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AM942759; CAR47188.1; -; Genomic_DNA.
DR   PIR; F43719; F43719.
DR   AlphaFoldDB; P17091; -.
DR   SMR; P17091; -.
DR   STRING; 529507.PMI3687; -.
DR   EnsemblBacteria; CAR47188; CAR47188; PMI3687.
DR   KEGG; pmr:PMI3687; -.
DR   eggNOG; COG0830; Bacteria.
DR   HOGENOM; CLU_049215_2_1_6; -.
DR   OMA; TQYTRLF; -.
DR   Proteomes; UP000008319; Chromosome.
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   Gene3D; 1.10.4190.10; -; 1.
DR   HAMAP; MF_01385; UreF; 1.
DR   InterPro; IPR002639; UreF.
DR   InterPro; IPR038277; UreF_sf.
DR   Pfam; PF01730; UreF; 1.
DR   PIRSF; PIRSF009467; Ureas_acces_UreF; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Nickel insertion; Reference proteome; Virulence.
FT   CHAIN           1..222
FT                   /note="Urease accessory protein UreF"
FT                   /id="PRO_0000067652"
FT   MUTAGEN         183
FT                   /note="I->IRRRI: Reduces urease activity 5-fold."
FT                   /evidence="ECO:0000269|PubMed:7559355"
FT   CONFLICT        100
FT                   /note="R -> P (in Ref. 1; AAA25671)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="A -> P (in Ref. 1; AAA25671)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   222 AA;  24993 MW;  005D6CA905A1E231 CRC64;
     MMLADLRLYQ LVSPSLPVGA FTYSQGLEWA IEKGWVCSAE TLSDWLSAQM TGTLATLELP
     ILRQLQTSLA KGDSDTVKYW CDFMVASRET KELRQEERQR GIAFARLLPQ LGIELDDTLQ
     QRVKQTQLMA FALAAVHWHI DSEKLCCAYV WGWLENTVMS GVKLVPLGQS AGQKMLFALA
     EQIPAIVELS AHWPQEDIGS FTPAQVIASS RHETQYTRLF RS