NANR_ECOLI
ID NANR_ECOLI Reviewed; 263 AA.
AC P0A8W0; P45427; Q2M8Y7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=HTH-type transcriptional repressor NanR {ECO:0000255|HAMAP-Rule:MF_01236, ECO:0000305};
GN Name=nanR {ECO:0000255|HAMAP-Rule:MF_01236, ECO:0000303|PubMed:9864311};
GN Synonyms=yhcK; OrderedLocusNames=b3226, JW3195;
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 / 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 [2]
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 [3]
RP FUNCTION.
RX PubMed=9864311; DOI=10.1128/jb.181.1.47-54.1999;
RA Plumbridge J., Vimr E.;
RT "Convergent pathways for utilization of the amino sugars N-
RT acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by
RT Escherichia coli.";
RL J. Bacteriol. 181:47-54(1999).
RN [4]
RP FUNCTION, DNA-BINDING, AND SUBUNIT.
RX PubMed=12897000; DOI=10.1128/jb.185.16.4806-4815.2003;
RA Kalivoda K.A., Steenbergen S.M., Vimr E.R., Plumbridge J.;
RT "Regulation of sialic acid catabolism by the DNA binding protein NanR in
RT Escherichia coli.";
RL J. Bacteriol. 185:4806-4815(2003).
RN [5]
RP FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=23935044; DOI=10.1128/jb.00692-13;
RA Kalivoda K.A., Steenbergen S.M., Vimr E.R.;
RT "Control of the Escherichia coli sialoregulon by transcriptional repressor
RT NanR.";
RL J. Bacteriol. 195:4689-4701(2013).
CC -!- FUNCTION: Transcriptional repressor that controls expression of the
CC genes required for the catabolism of sialic acids (PubMed:9864311,
CC PubMed:12897000, PubMed:23935044). Represses expression of the nanATEK-
CC yhcH, nanCMS and yjhBC operons. Acts by binding directly to the Nan
CC box, a region of approximately 30 bp covering the promoter region
CC (PubMed:23935044). {ECO:0000269|PubMed:12897000,
CC ECO:0000269|PubMed:23935044, ECO:0000269|PubMed:9864311}.
CC -!- ACTIVITY REGULATION: N-acetylneuraminic acid (Neu5Ac) inactivates NanR
CC by converting NanR oligomers to monomers.
CC {ECO:0000269|PubMed:23935044}.
CC -!- SUBUNIT: Homodimer (PubMed:12897000, PubMed:23935044). Might also form
CC higher-order oligomers (PubMed:23935044). {ECO:0000269|PubMed:12897000,
CC ECO:0000269|PubMed:23935044}.
CC -!- SIMILARITY: Belongs to the NanR family. {ECO:0000255|HAMAP-
CC Rule:MF_01236, ECO:0000305}.
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DR EMBL; U18997; AAA58028.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76258.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77269.1; -; Genomic_DNA.
DR PIR; D65114; D65114.
DR RefSeq; NP_417693.3; NC_000913.3.
DR RefSeq; WP_000523845.1; NZ_STEB01000012.1.
DR PDB; 6ON4; X-ray; 2.10 A; A/B=1-263.
DR PDB; 6WFQ; EM; 3.90 A; C/D=1-263.
DR PDB; 6WG7; EM; 8.30 A; C/D/E/F/G/H=1-263.
DR PDBsum; 6ON4; -.
DR PDBsum; 6WFQ; -.
DR PDBsum; 6WG7; -.
DR AlphaFoldDB; P0A8W0; -.
DR SASBDB; P0A8W0; -.
DR SMR; P0A8W0; -.
DR BioGRID; 4262443; 14.
DR DIP; DIP-12284N; -.
DR IntAct; P0A8W0; 1.
DR STRING; 511145.b3226; -.
DR jPOST; P0A8W0; -.
DR PaxDb; P0A8W0; -.
DR PRIDE; P0A8W0; -.
DR EnsemblBacteria; AAC76258; AAC76258; b3226.
DR EnsemblBacteria; BAE77269; BAE77269; BAE77269.
DR GeneID; 66672878; -.
DR GeneID; 945468; -.
DR KEGG; ecj:JW3195; -.
DR KEGG; eco:b3226; -.
DR PATRIC; fig|1411691.4.peg.3502; -.
DR EchoBASE; EB2668; -.
DR eggNOG; COG2186; Bacteria.
DR HOGENOM; CLU_017584_9_1_6; -.
DR InParanoid; P0A8W0; -.
DR OMA; HDAFVDW; -.
DR PhylomeDB; P0A8W0; -.
DR BioCyc; EcoCyc:G7678-MON; -.
DR PRO; PR:P0A8W0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.120.530; -; 1.
DR HAMAP; MF_01236; HTH_NanR; 1.
DR InterPro; IPR011711; GntR_C.
DR InterPro; IPR008920; TF_FadR/GntR_C.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR023730; Tscrpt_reg_NanR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF07729; FCD; 1.
DR Pfam; PF00392; GntR; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00895; FCD; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48008; SSF48008; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..263
FT /note="HTH-type transcriptional repressor NanR"
FT /id="PRO_0000050655"
FT DOMAIN 30..98
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01236"
FT DNA_BIND 58..77
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01236"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:6ON4"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:6ON4"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:6ON4"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:6ON4"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 186..202
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 208..230
FT /evidence="ECO:0007829|PDB:6ON4"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:6ON4"
SQ SEQUENCE 263 AA; 29524 MW; 306B3D8FAD7D8BB6 CRC64;
MGLMNAFDSQ TEDSSPAIGR NLRSRPLARK KLSEMVEEEL EQMIRRREFG EGEQLPSERE
LMAFFNVGRP SVREALAALK RKGLVQINNG ERARVSRPSA DTIIGELSGM AKDFLSHPGG
IAHFEQLRLF FESSLVRYAA EHATDEQIDL LAKALEINSQ SLDNNAAFIR SDVDFHRVLA
EIPGNPIFMA IHVALLDWLI AARPTVTDQA LHEHNNVSYQ QHIAIVDAIR RHDPDEADRA
LQSHLNSVSA TWHAFGQTTN KKK
