ID   MNTR_ECOL6              Reviewed;         155 AA.
AC   P0A9F2; P75787;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Transcriptional regulator MntR;
DE   AltName: Full=Manganese transport regulator;
GN   Name=mntR; OrderedLocusNames=c0903;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: In the presence of manganese, represses expression of mntH
CC       and mntS. Up-regulates expression of mntP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: It contains an N-terminal DNA-binding domain and a metal-
CC       binding domain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DtxR/MntR family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN79376.1; -; Genomic_DNA.
DR   RefSeq; WP_000091016.1; NC_004431.1.
DR   AlphaFoldDB; P0A9F2; -.
DR   SMR; P0A9F2; -.
DR   STRING; 199310.c0903; -.
DR   EnsemblBacteria; AAN79376; AAN79376; c0903.
DR   GeneID; 67413856; -.
DR   KEGG; ecc:c0903; -.
DR   eggNOG; COG1321; Bacteria.
DR   HOGENOM; CLU_069532_2_0_6; -.
DR   OMA; SWDAIDR; -.
DR   BioCyc; ECOL199310:C0903-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.60.10; -; 1.
DR   InterPro; IPR001367; Fe_dep_repressor.
DR   InterPro; IPR036421; Fe_dep_repressor_sf.
DR   InterPro; IPR022687; HTH_DTXR.
DR   InterPro; IPR022689; Iron_dep_repressor.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF02742; Fe_dep_repr_C; 1.
DR   Pfam; PF01325; Fe_dep_repress; 1.
DR   SMART; SM00529; HTH_DTXR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47979; SSF47979; 1.
DR   PROSITE; PS50944; HTH_DTXR; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Manganese; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..155
FT                   /note="Transcriptional regulator MntR"
FT                   /id="PRO_0000201112"
FT   DOMAIN          34..95
FT                   /note="HTH dtxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00296"
SQ   SEQUENCE   155 AA;  17640 MW;  CB316AC7F1BDD106 CRC64;
     MSRRAGTPTA KKVTQLVNVE EHVEGFRQVR EAHRRELIDD YVELISDLIR EVGEARQVDM
     AARLGVSQPT VAKMLKRLAT MGLIEMIPWR GVFLTAEGEK LAQESRERHQ IVENFLLVLG
     VSPEIARRDA EGMEHHVSEE TLDAFRLFTQ KHGAK