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Database: UniProt
Entry: U2C3H6_9FLAO
LinkDB: U2C3H6_9FLAO
Original site: U2C3H6_9FLAO 
ID   U2C3H6_9FLAO            Unreviewed;       218 AA.
AC   U2C3H6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Manganese transport regulator {ECO:0000256|ARBA:ARBA00032593};
GN   ORFNames=HMPREF1551_02155 {ECO:0000313|EMBL:ERI61941.1};
OS   Capnocytophaga sp. oral taxon 863 str. F0517.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1227266 {ECO:0000313|EMBL:ERI61941.1, ECO:0000313|Proteomes:UP000016494};
RN   [1] {ECO:0000313|EMBL:ERI61941.1, ECO:0000313|Proteomes:UP000016494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0517 {ECO:0000313|EMBL:ERI61941.1,
RC   ECO:0000313|Proteomes:UP000016494};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DtxR/MntR family.
CC       {ECO:0000256|ARBA:ARBA00007871}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERI61941.1}.
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DR   EMBL; AWSR01000156; ERI61941.1; -; Genomic_DNA.
DR   RefSeq; WP_021628900.1; NZ_KE992171.1.
DR   AlphaFoldDB; U2C3H6; -.
DR   STRING; 1227266.HMPREF1551_02155; -.
DR   PATRIC; fig|1227266.3.peg.1918; -.
DR   eggNOG; COG1321; Bacteria.
DR   HOGENOM; CLU_069532_0_2_10; -.
DR   OrthoDB; 9791355at2; -.
DR   Proteomes; UP000016494; Unassembled WGS sequence.
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; 2.30.30.90; -; 1.
DR   Gene3D; 1.10.60.10; Iron dependent repressor, metal binding and dimerisation domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR007167; Fe-transptr_FeoA.
DR   InterPro; IPR001367; Fe_dep_repressor.
DR   InterPro; IPR036421; Fe_dep_repressor_sf.
DR   InterPro; IPR038157; FeoA_core_dom.
DR   InterPro; IPR022687; HTH_DTXR.
DR   InterPro; IPR022689; Iron_dep_repressor.
DR   InterPro; IPR008988; Transcriptional_repressor_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR33238; IRON (METAL) DEPENDENT REPRESSOR, DTXR FAMILY; 1.
DR   PANTHER; PTHR33238:SF7; TRANSCRIPTIONAL REGULATOR MNTR; 1.
DR   Pfam; PF02742; Fe_dep_repr_C; 1.
DR   Pfam; PF01325; Fe_dep_repress; 1.
DR   Pfam; PF04023; FeoA; 1.
DR   SMART; SM00899; FeoA; 1.
DR   SMART; SM00529; HTH_DTXR; 1.
DR   SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR   SUPFAM; SSF47979; Iron-dependent repressor protein, dimerization domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50944; HTH_DTXR; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1..63
FT                   /note="HTH dtxR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50944"
SQ   SEQUENCE   218 AA;  25265 MW;  94E388E0B293FDF6 CRC64;
     MTFSEENYLK IIYHLGQERQ EEVTTNAIAE AIQTKASSVT DMLKKLHEKG WVEHKKYQGV
     SLTKEGAKNA LLVIRKHRLW EVFLVEKLHF SWDEVHEVAE QLEHIQSDKL IEELDKLLLY
     PEKDPHGDPI PDKYGHMPTL KSELLSHMKK DEVAQCIGVK NTSKEFLQYL NKIDISIGKE
     IKILEIHPFD NSIEIQLDSH SINISSIVAE NIYVKKNK
//
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