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MNTR_ECOLI
ID   MNTR_ECOLI              Reviewed;         155 AA.
AC   P0A9F1; P75787;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Transcriptional regulator MntR;
DE   AltName: Full=Manganese transport regulator;
GN   Name=mntR; Synonyms=ybiQ; OrderedLocusNames=b0817, JW0801;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, AND DNA-BINDING.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=11466284; DOI=10.1128/jb.183.16.4806-4813.2001;
RA   Patzer S.I., Hantke K.;
RT   "Dual repression by Fe(2+)-Fur and Mn(2+)-MntR of the mntH gene, encoding
RT   an NRAMP-like Mn(2+) transporter in Escherichia coli.";
RL   J. Bacteriol. 183:4806-4813(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=21908668; DOI=10.1128/jb.05872-11;
RA   Waters L.S., Sandoval M., Storz G.;
RT   "The Escherichia coli MntR miniregulon includes genes encoding a small
RT   protein and an efflux pump required for manganese homeostasis.";
RL   J. Bacteriol. 193:5887-5897(2011).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT, AND DOMAIN.
RC   STRAIN=K12;
RX   PubMed=19701940; DOI=10.1002/prot.22541;
RA   Tanaka T., Shinkai A., Bessho Y., Kumarevel T., Yokoyama S.;
RT   "Crystal structure of the manganese transport regulatory protein from
RT   Escherichia coli.";
RL   Proteins 77:741-746(2009).
CC   -!- FUNCTION: In the presence of manganese, represses expression of mntH
CC       and mntS. Up-regulates expression of mntP.
CC       {ECO:0000269|PubMed:11466284, ECO:0000269|PubMed:21908668}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19701940}.
CC   -!- INTERACTION:
CC       P0A9F1; P16433: hycG; NbExp=4; IntAct=EBI-541895, EBI-541977;
CC       P0A9F1; P30750: metN; NbExp=4; IntAct=EBI-541895, EBI-541886;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: It contains an N-terminal DNA-binding domain and a metal-
CC       binding domain. {ECO:0000269|PubMed:19701940}.
CC   -!- SIMILARITY: Belongs to the DtxR/MntR family. {ECO:0000305}.
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DR   EMBL; U00096; AAC73904.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35488.1; -; Genomic_DNA.
DR   PIR; A64819; A64819.
DR   RefSeq; NP_415338.1; NC_000913.3.
DR   RefSeq; WP_000091016.1; NZ_STEB01000019.1.
DR   PDB; 2H09; X-ray; 2.10 A; A=1-155.
DR   PDBsum; 2H09; -.
DR   AlphaFoldDB; P0A9F1; -.
DR   SMR; P0A9F1; -.
DR   BioGRID; 4261205; 12.
DR   BioGRID; 849811; 7.
DR   DIP; DIP-28083N; -.
DR   IntAct; P0A9F1; 10.
DR   STRING; 511145.b0817; -.
DR   jPOST; P0A9F1; -.
DR   PaxDb; P0A9F1; -.
DR   PRIDE; P0A9F1; -.
DR   EnsemblBacteria; AAC73904; AAC73904; b0817.
DR   EnsemblBacteria; BAA35488; BAA35488; BAA35488.
DR   GeneID; 67413856; -.
DR   GeneID; 945437; -.
DR   KEGG; ecj:JW0801; -.
DR   KEGG; eco:b0817; -.
DR   PATRIC; fig|1411691.4.peg.1461; -.
DR   EchoBASE; EB3106; -.
DR   eggNOG; COG1321; Bacteria.
DR   HOGENOM; CLU_069532_2_0_6; -.
DR   InParanoid; P0A9F1; -.
DR   OMA; SWDAIDR; -.
DR   PhylomeDB; P0A9F1; -.
DR   BioCyc; EcoCyc:G6420-MON; -.
DR   EvolutionaryTrace; P0A9F1; -.
DR   PRO; PR:P0A9F1; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   CollecTF; EXPREG_000007f0; -.
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; IDA:EcoCyc.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR   GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IEP:EcoCyc.
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   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; DNA-binding; Manganese;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..155
FT                   /note="Transcriptional regulator MntR"
FT                   /id="PRO_0000201110"
FT   DOMAIN          34..95
FT                   /note="HTH dtxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00296"
FT   HELIX           27..52
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   HELIX           57..64
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   HELIX           68..80
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   HELIX           96..119
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   HELIX           123..133
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:2H09"
FT   HELIX           139..147
FT                   /evidence="ECO:0007829|PDB:2H09"
SQ   SEQUENCE   155 AA;  17640 MW;  CB316AC7F1BDD106 CRC64;
     MSRRAGTPTA KKVTQLVNVE EHVEGFRQVR EAHRRELIDD YVELISDLIR EVGEARQVDM
     AARLGVSQPT VAKMLKRLAT MGLIEMIPWR GVFLTAEGEK LAQESRERHQ IVENFLLVLG
     VSPEIARRDA EGMEHHVSEE TLDAFRLFTQ KHGAK
 
 
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