Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A9E5

- FNR_ECOLI

UniProt

P0A9E5 - FNR_ECOLI

Protein

Fumarate and nitrate reduction regulatory protein

Gene

fnr

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O2, is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration.

    Cofactori

    Binds 1 4Fe-4S cluster per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi20 – 201Iron-sulfur (4Fe-4S)Sequence Analysis
    Metal bindingi23 – 231Iron-sulfur (4Fe-4S)Sequence Analysis
    Metal bindingi29 – 291Iron-sulfur (4Fe-4S)Sequence Analysis
    Metal bindingi122 – 1221Iron-sulfur (4Fe-4S)Sequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi197 – 21620H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: EcoCyc
    2. DNA binding Source: EcoCyc
    3. iron-sulfur cluster binding Source: EcoCyc
    4. metal ion binding Source: UniProtKB-KW
    5. sequence-specific DNA binding transcription factor activity Source: EcoCyc

    GO - Biological processi

    1. anaerobic respiration Source: EcoCyc
    2. regulation of transcription, DNA-templated Source: EcoCyc
    3. response to nitric oxide Source: EcoCyc
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PD00197.
    ECOL316407:JW1328-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate and nitrate reduction regulatory protein
    Gene namesi
    Name:fnr
    Synonyms:nirR
    Ordered Locus Names:b1334, JW1328
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10325. fnr.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161C → A: No effect. 1 Publication
    Mutagenesisi20 – 201C → S: Loss of activity. 1 Publication
    Mutagenesisi22 – 221D → G: Loss of regulation by O(2). 1 Publication
    Mutagenesisi23 – 231C → G: Loss of activity. 1 Publication
    Mutagenesisi28 – 281L → H: Loss of regulation by O(2). 1 Publication
    Mutagenesisi29 – 291C → G: Loss of activity. 1 Publication
    Mutagenesisi43 – 431D → G: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi64 – 641E → Q: No effect. 1 Publication
    Mutagenesisi72 – 721R → H: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi73 – 731S → F: Decrease in activity; no effect on DNA-binding. 2 Publications
    Mutagenesisi81 – 811I → T: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi82 – 821T → P: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi85 – 851G → A: Decrease in activity; no effect on DNA-binding. Trace activity; when associated with P-187. 2 Publications
    Mutagenesisi86 – 861D → A: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi87 – 871E → K: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi88 – 881Q → E: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi93 – 931H → R: Loss of regulation by O(2). 1 Publication
    Mutagenesisi96 – 961G → D: Loss of activity. 1 Publication
    Mutagenesisi118 – 1181T → A or P: Decrease in activity; no effect on DNA-binding. 2 Publications
    Mutagenesisi120 – 1201M → I, R, T or V: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi122 – 1221C → A or S: Loss of activity. 1 Publication
    Mutagenesisi140 – 1401R → A: Decrease in activity.
    Mutagenesisi143 – 1431M → A: Decrease in activity.
    Mutagenesisi144 – 1441M → A: Decrease in activity due to faulty dimerization.
    Mutagenesisi145 – 1451R → A: Decrease in activity.
    Mutagenesisi146 – 1461L → A: Decrease in activity.
    Mutagenesisi147 – 1471M → A: Decrease in activity due to faulty dimerization.
    Mutagenesisi150 – 1501E → K: Loss of regulation by O(2). 1 Publication
    Mutagenesisi151 – 1511I → A: Decrease in activity due to faulty dimerization.
    Mutagenesisi154 – 1541D → A, G or V: Loss of regulation by O(2). 2 Publications
    Mutagenesisi158 – 1581I → A: Decrease in activity due to faulty dimerization.
    Mutagenesisi181 – 1811F → L: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi186 – 1861F → S: Decrease in activity; no effect on DNA-binding. 1 Publication
    Mutagenesisi187 – 1871S → P: Decrease in activity; no effect on DNA-binding. Trace activity; when associated with A-85. 2 Publications
    Mutagenesisi191 – 1911F → L: Decrease in activity; no effect on DNA-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 250250Fumarate and nitrate reduction regulatory proteinPRO_0000100161Add
    BLAST

    Proteomic databases

    PaxDbiP0A9E5.
    PRIDEiP0A9E5.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9E5.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-9669N.
    IntActiP0A9E5. 8 interactions.
    MINTiMINT-1237977.
    STRINGi511145.b1334.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A9E5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini164 – 23774HTH crp-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 2910Essential for the oxygen-regulated activity
    Regioni47 – 504Activating region 2ASequence Analysis
    Regioni60 – 612Activating region 3ASequence Analysis
    Regioni71 – 755Activating region 1ASequence Analysis
    Regioni81 – 811Activating region 3BSequence Analysis
    Regioni85 – 873Activating region 3CSequence Analysis
    Regioni112 – 1121Activating region 3DSequence Analysis
    Regioni116 – 1216Activating region 1BSequence Analysis
    Regioni123 – 1242Activating region 2BSequence Analysis
    Regioni127 – 1282Activating region 2CSequence Analysis
    Regioni140 – 15920DimerizationSequence AnalysisAdd
    BLAST
    Regioni181 – 19111Activating region 1CSequence AnalysisAdd
    BLAST

    Domaini

    The amino acid residues contacting the FNR target site on the DNA (5'-TTGATNNNNATCAA-3') are located in the putative DNA-recognition helix (alphaF), which contains the FNR motif (EXXSR). Three surface-exposed loops forming activating region 1 (AR1) in the downstream subunit of the dimer contact the C-terminal domain of the alpha subunit (alphaCTD) of RNA polymerase for activation of class I promoters (the 161-121 loop is the major AR1 activating determinant). At class II promoters, the AR1 of the upstream subunit contacts alphaCTD, promoting open complex formation; activating region 3 (AR3) of the downstream subunit contacts region 4 of the sigma70 subunit of RNA polymerase, to effect direct activation. At promoters repressed by FNR, tandem FNR dimers might interact with each other at AR1 to restrict access to a promoter or jam the promoter by their dual interaction with RNA polymerase alphaCTD.

    Sequence similaritiesi

    Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
    Contains 1 HTH crp-type DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0664.
    HOGENOMiHOG000186461.
    KOiK01420.
    OMAiFSANQFR.
    OrthoDBiEOG6RVFWF.
    PhylomeDBiP0A9E5.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.60.120.10. 1 hit.
    InterProiIPR018490. cNMP-bd-like.
    IPR000595. cNMP-bd_dom.
    IPR012318. HTH_CRP_2.
    IPR014710. RmlC-like_jellyroll.
    IPR001808. Tscrpt_reg_HTH_Crp.
    IPR018335. Tscrpt_reg_HTH_Crp-type_CS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00027. cNMP_binding. 1 hit.
    PF00325. Crp. 1 hit.
    [Graphical view]
    PRINTSiPR00034. HTHCRP.
    SMARTiSM00100. cNMP. 1 hit.
    SM00419. HTH_CRP. 1 hit.
    [Graphical view]
    SUPFAMiSSF51206. SSF51206. 1 hit.
    PROSITEiPS50042. CNMP_BINDING_3. 1 hit.
    PS00042. HTH_CRP_1. 1 hit.
    PS51063. HTH_CRP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A9E5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIPEKRIIRR IQSGGCAIHC QDCSISQLCI PFTLNEHELD QLDNIIERKK    50
    PIQKGQTLFK AGDELKSLYA IRSGTIKSYT ITEQGDEQIT GFHLAGDLVG 100
    FDAIGSGHHP SFAQALETSM VCEIPFETLD DLSGKMPNLR QQMMRLMSGE 150
    IKGDQDMILL LSKKNAEERL AAFIYNLSRR FAQRGFSPRE FRLTMTRGDI 200
    GNYLGLTVET ISRLLGRFQK SGMLAVKGKY ITIENNDALA QLAGHTRNVA 250
    Length:250
    Mass (Da):27,967
    Last modified:July 19, 2005 - v1
    Checksum:i33F7BFA2972FF703
    GO

    Mass spectrometryi

    Molecular mass is 26823±6 Da from positions 10 - 250. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01608 Genomic DNA. Translation: AAA87981.1. Sequence problems.
    U00096 Genomic DNA. Translation: AAC74416.1.
    AP009048 Genomic DNA. Translation: BAA14927.1.
    PIRiA64883. RGECF.
    RefSeqiNP_415850.1. NC_000913.3.
    YP_489604.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74416; AAC74416; b1334.
    BAA14927; BAA14927; BAA14927.
    GeneIDi12932858.
    945908.
    KEGGiecj:Y75_p1311.
    eco:b1334.
    PATRICi32117944. VBIEscCol129921_1392.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01608 Genomic DNA. Translation: AAA87981.1 . Sequence problems.
    U00096 Genomic DNA. Translation: AAC74416.1 .
    AP009048 Genomic DNA. Translation: BAA14927.1 .
    PIRi A64883. RGECF.
    RefSeqi NP_415850.1. NC_000913.3.
    YP_489604.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0A9E5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9669N.
    IntActi P0A9E5. 8 interactions.
    MINTi MINT-1237977.
    STRINGi 511145.b1334.

    Proteomic databases

    PaxDbi P0A9E5.
    PRIDEi P0A9E5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74416 ; AAC74416 ; b1334 .
    BAA14927 ; BAA14927 ; BAA14927 .
    GeneIDi 12932858.
    945908.
    KEGGi ecj:Y75_p1311.
    eco:b1334.
    PATRICi 32117944. VBIEscCol129921_1392.

    Organism-specific databases

    EchoBASEi EB0321.
    EcoGenei EG10325. fnr.

    Phylogenomic databases

    eggNOGi COG0664.
    HOGENOMi HOG000186461.
    KOi K01420.
    OMAi FSANQFR.
    OrthoDBi EOG6RVFWF.
    PhylomeDBi P0A9E5.

    Enzyme and pathway databases

    BioCyci EcoCyc:PD00197.
    ECOL316407:JW1328-MONOMER.

    Miscellaneous databases

    PROi P0A9E5.

    Gene expression databases

    Genevestigatori P0A9E5.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.60.120.10. 1 hit.
    InterProi IPR018490. cNMP-bd-like.
    IPR000595. cNMP-bd_dom.
    IPR012318. HTH_CRP_2.
    IPR014710. RmlC-like_jellyroll.
    IPR001808. Tscrpt_reg_HTH_Crp.
    IPR018335. Tscrpt_reg_HTH_Crp-type_CS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00027. cNMP_binding. 1 hit.
    PF00325. Crp. 1 hit.
    [Graphical view ]
    PRINTSi PR00034. HTHCRP.
    SMARTi SM00100. cNMP. 1 hit.
    SM00419. HTH_CRP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51206. SSF51206. 1 hit.
    PROSITEi PS50042. CNMP_BINDING_3. 1 hit.
    PS00042. HTH_CRP_1. 1 hit.
    PS51063. HTH_CRP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the fnr gene and primary structure of the Enr protein of Escherichia coli."
      Shaw D.J., Guest J.R.
      Nucleic Acids Res. 10:6119-6130(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Isolation of intact FNR protein (Mr 30,000) of Escherichia coli."
      Trageser M., Spiro S., Duchene A., Kojro E., Fahrenholz F., Guest J.R., Unden G.
      Mol. Microbiol. 4:21-27(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-19, SEQUENCE REVISION TO 29.
    6. "The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state."
      Lazazzera B.A., Bates D.M., Kiley P.J.
      Genes Dev. 7:1993-2005(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-154.
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity."
      Khoroshilova N., Popescu C., Muenck E., Beinert H., Kiley P.J.
      Proc. Natl. Acad. Sci. U.S.A. 94:6087-6092(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: B.
    8. "Anaerobic acquisition of [4FE 4S] clusters by the inactive FNR(C20S) variant and restoration of activity by second-site amino acid substitutions."
      Ralph E.T., Scott C., Jordan P.A., Thomson A.J., Guest J.R., Green J.
      Mol. Microbiol. 39:1199-1211(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS.
    9. "Properties of FNR proteins substituted at each of the five cysteine residues."
      Green J., Sharrocks A.D., Green B., Geisow M., Guest J.R.
      Mol. Microbiol. 8:61-68(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY, CHARACTERIZATION OF MUTANTS.
    10. "In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of E. coli."
      Sharrocks A.D., Green J., Guest J.R.
      FEBS Lett. 270:119-122(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-16; CYS-20; CYS-23; CYS-29; GLU-64; GLY-96 AND CYS-122.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    11. "Fnr mutants that activate gene expression in the presence of oxygen."
      Kiley P.J., Reznikoff W.S.
      J. Bacteriol. 173:16-22(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-22; LEU-28; HIS-93; GLU-150 AND ASP-154.
      Strain: K12 / MG1655 / ATCC 47076.
    12. "The role of two surface exposed loops in transcription activation by the Escherichia coli CRP and FNR proteins."
      Williams R., Bell A., Sims G., Busby S.J.W.
      Nucleic Acids Res. 19:6705-6712(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ILE-81; THR-82; GLY-85; ASP-86; GLU-87 AND GLN-88.
    13. "Transcription activation at class I FNR-dependent promoters: identification of the activating surface of FNR and the corresponding contact site in the C-terminal domain of the RNA polymerase alpha subunit."
      Williams S.M., Savery N.J., Busby S.J.W., Wing H.J.
      Nucleic Acids Res. 25:4028-4034(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-43; ARG-72; SER-73; GLY-74; THR-118; MET-120; PHE-181; PHE-186; SER-187 AND PHE-191.
    14. "FNR-dependent activation of the class II dmsA and narG promoters of Escherichia coli requires FNR-activating regions 1 and 3."
      Lamberg K.E., Kiley P.J.
      Mol. Microbiol. 38:817-827(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-73; GLY-85; THR-118 AND SER-187.
      Strain: K12 / MG1655 / ATCC 47076.
    15. "Characterization of the dimerization domain in the FNR transcription factor."
      Moore L.J., Kiley P.J.
      J. Biol. Chem. 276:45744-45750(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ALL RESIDUES IN THE DIMERIZATION HELIX.
      Strain: K12 / MG1655 / ATCC 47076.
    16. "FNR and its role in oxygen-regulated gene expression in Escherichia coli."
      Spiro S., Guest J.R.
      FEMS Microbiol. Rev. 6:399-428(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    17. "Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster."
      Kiley P.J., Beinert H.
      FEMS Microbiol. Rev. 22:341-352(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. "Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP."
      Green J., Scott C., Guest J.R.
      Adv. Microb. Physiol. 44:1-34(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiFNR_ECOLI
    AccessioniPrimary (citable) accession number: P0A9E5
    Secondary accession number(s): P03019
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    FNR senses the oxygen concentration directly via the disassembly and reassembly of the [4Fe-4S] clusters. Anaerobic, de novo acquisition of the iron-sulfur cluster converts monomeric, inactive apo-FNR into a dimeric form containing two [4Fe-4S] clusters. This, in turn, enhances the affinity of FNR for specific DNA targets and mediates transcription regulation by establishing direct FNR-RNA polymerase contacts. With the increase in intracellular oxygen concentration, the [4Fe-4S] cluster is oxidized, producing a [2Fe-2S] cluster, which decays to apo-FNR. Apo-FNR [4SH] can be reversibly oxidized to a disulfide form [2SH,S-S], suggesting that FNR may be able to sense oxidative stress as well as normoxia. This interconversion may be mediated by agents such as glutathione or thioredoxin.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3