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P0ACF8

- HNS_ECOLI

UniProt

P0ACF8 - HNS_ECOLI

Protein

DNA-binding protein H-NS

Gene

hns

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    A DNA-binding protein implicated in transcriptional repression (silencing) as well as in bacterial chromosome organization. H-NS binds tightly to AT-rich dsDNA, increases its thermal stability and inhibits transcription. Also binds to ssDNA and RNA but with a much lower affinity. H-NS has possible histone-like function. May be a global transcriptional regulator through its ability to bind to curved DNA sequences, which are found in regions upstream of a certain subset of promoters. Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD. Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its role is antagonized by LeuO. Subject to transcriptional auto-repression. Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei12 – 121Interacts with Hha

    GO - Molecular functioni

    1. bent DNA binding Source: EcoliWiki
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PD00288.
    ECOL316407:JW1225-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-binding protein H-NS
    Alternative name(s):
    Histone-like protein HLP-II
    Protein B1
    Protein H1
    Gene namesi
    Name:hns
    Synonyms:bglY, cur, drdX, hnsA, msyA, osmZ, pilG, topS
    Ordered Locus Names:b1237, JW1225
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10457. hns.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: InterPro
    2. membrane Source: UniProtKB

    Pathology & Biotechi

    Disruption phenotypei

    At 28 degrees Celsius csgD transcription is reduced. Flagella loss due to reduced expression of the flhDC operon. Flagella can be restored by expression of flhDC, but strains are non-motile, suggesting H-NS also plays a role in flagellar function. Disruption leads to increased expression of CRISPR-cas genes and increased viral resistance.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121R → K: Abolishes the interaction with Hha. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed7 Publications
    Chaini2 – 137136DNA-binding protein H-NSPRO_0000168503Add
    BLAST

    Proteomic databases

    PaxDbiP0ACF8.
    PRIDEiP0ACF8.

    2D gel databases

    SWISS-2DPAGEP0ACF8.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ACF8.

    Interactioni

    Subunit structurei

    Homodimer, it can multimerize into higher-order complexes that form bridges between adjacent DNA helices. Can form a complex with Cnu and with Hha.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself10EBI-544934,EBI-544934
    cnuP644672EBI-544934,EBI-551907
    hhaP0ACE35EBI-544934,EBI-1122578
    stpAP0ACG13EBI-544934,EBI-551928

    Protein-protein interaction databases

    BioGridi850196. 1 interaction.
    DIPiDIP-35853N.
    IntActiP0ACF8. 49 interactions.
    MINTiMINT-1223907.
    STRINGi511145.b1237.

    Structurei

    Secondary structure

    1
    137
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 75
    Helixi10 – 178
    Turni18 – 203
    Helixi24 – 5128
    Beta strandi97 – 993
    Beta strandi100 – 1067
    Turni110 – 1134
    Beta strandi115 – 1173
    Helixi118 – 1258
    Helixi130 – 1323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HNRNMR-A91-137[»]
    1HNSNMR-A91-137[»]
    1LR1NMR-A/B2-58[»]
    1NI8NMR-A/B2-47[»]
    ProteinModelPortaliP0ACF8.
    SMRiP0ACF8. Positions 2-81, 91-137.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ACF8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone-like protein H-NS family.Curated

    Phylogenomic databases

    eggNOGiCOG2916.
    HOGENOMiHOG000218473.
    KOiK03746.
    OMAiNGENKTW.
    OrthoDBiEOG6NPM97.

    Family and domain databases

    Gene3Di1.10.287.1050. 1 hit.
    4.10.430.10. 1 hit.
    InterProiIPR027444. H-NS_C_dom.
    IPR001801. Histone_HNS.
    IPR027454. Histone_HNS_oligo_dom.
    [Graphical view]
    PfamiPF00816. Histone_HNS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002096. HnS. 1 hit.
    SMARTiSM00528. HNS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0ACF8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE    50
    VEERTRKLQQ YREMLIADGI DPNELLNSLA AVKSGTKAKR AQRPAKYSYV 100
    DENGETKTWT GQGRTPAVIK KAMDEQGKSL DDFLIKQ 137
    Length:137
    Mass (Da):15,540
    Last modified:January 23, 2007 - v2
    Checksum:iE628184AC7C86F49
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07688 Genomic DNA. Translation: CAA30530.1.
    X59940 Genomic DNA. Translation: CAA42565.1.
    X57231 Genomic DNA. Translation: CAA40507.1.
    X67326 Genomic DNA. Translation: CAA47740.1.
    U00096 Genomic DNA. Translation: AAC74319.1.
    AP009048 Genomic DNA. Translation: BAA36117.1.
    PIRiS00903.
    RefSeqiNP_415753.1. NC_000913.3.
    YP_489505.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74319; AAC74319; b1237.
    BAA36117; BAA36117; BAA36117.
    GeneIDi12934502.
    945829.
    KEGGiecj:Y75_p1210.
    eco:b1237.
    PATRICi32117730. VBIEscCol129921_1285.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07688 Genomic DNA. Translation: CAA30530.1 .
    X59940 Genomic DNA. Translation: CAA42565.1 .
    X57231 Genomic DNA. Translation: CAA40507.1 .
    X67326 Genomic DNA. Translation: CAA47740.1 .
    U00096 Genomic DNA. Translation: AAC74319.1 .
    AP009048 Genomic DNA. Translation: BAA36117.1 .
    PIRi S00903.
    RefSeqi NP_415753.1. NC_000913.3.
    YP_489505.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HNR NMR - A 91-137 [» ]
    1HNS NMR - A 91-137 [» ]
    1LR1 NMR - A/B 2-58 [» ]
    1NI8 NMR - A/B 2-47 [» ]
    ProteinModelPortali P0ACF8.
    SMRi P0ACF8. Positions 2-81, 91-137.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 850196. 1 interaction.
    DIPi DIP-35853N.
    IntActi P0ACF8. 49 interactions.
    MINTi MINT-1223907.
    STRINGi 511145.b1237.

    2D gel databases

    SWISS-2DPAGE P0ACF8.

    Proteomic databases

    PaxDbi P0ACF8.
    PRIDEi P0ACF8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74319 ; AAC74319 ; b1237 .
    BAA36117 ; BAA36117 ; BAA36117 .
    GeneIDi 12934502.
    945829.
    KEGGi ecj:Y75_p1210.
    eco:b1237.
    PATRICi 32117730. VBIEscCol129921_1285.

    Organism-specific databases

    EchoBASEi EB0452.
    EcoGenei EG10457. hns.

    Phylogenomic databases

    eggNOGi COG2916.
    HOGENOMi HOG000218473.
    KOi K03746.
    OMAi NGENKTW.
    OrthoDBi EOG6NPM97.

    Enzyme and pathway databases

    BioCyci EcoCyc:PD00288.
    ECOL316407:JW1225-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ACF8.
    PROi P0ACF8.

    Gene expression databases

    Genevestigatori P0ACF8.

    Family and domain databases

    Gene3Di 1.10.287.1050. 1 hit.
    4.10.430.10. 1 hit.
    InterProi IPR027444. H-NS_C_dom.
    IPR001801. Histone_HNS.
    IPR027454. Histone_HNS_oligo_dom.
    [Graphical view ]
    Pfami PF00816. Histone_HNS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002096. HnS. 1 hit.
    SMARTi SM00528. HNS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification, cloning, nucleotide sequence and chromosomal map location of hns, the structural gene for Escherichia coli DNA-binding protein H-NS."
      Pon C.L., Calogero R.A., Gualerzi C.O.
      Mol. Gen. Genet. 212:199-202(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Transcriptional silencing and thermoregulation of gene expression in Escherichia coli."
      Goeransson M., Sonden B., Nilsson P., Dagberg B., Forsman K., Emanuelsson K., Uhlin B.E.
      Nature 344:682-685(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kD Escherichia coli DNA binding protein H-NS."
      Falconi M., Gualtieri M.T., la Teana A., Losso M.A., Pon C.L.
      Mol. Microbiol. 2:323-329(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Multicopy suppression: an approach to understanding intracellular functioning of the protein export system."
      Ueguchi C., Ito K.
      J. Bacteriol. 174:1454-1461(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    5. "The osmZ (bglY) gene encodes the DNA-binding protein H-NS (H1a), a component of the Escherichia coli K12 nucleoid."
      May G., Dersch P., Haardt M., Middendorf A., Bremer E.
      Mol. Gen. Genet. 224:81-90(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    8. "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.
    9. "Filling the gap between hns and adhE in Escherichia coli K12."
      Danchin A., Krin E.
      Microbiology 141:959-960(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
      Strain: K12.
    10. "Identification and sequence determination of the host factor gene for bacteriophage Q beta."
      Kajitani M., Ishihama A.
      Nucleic Acids Res. 19:1063-1066(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-27.
    11. "A DNA-binding protein from E. coli isolation, characterization and its relationship with proteins H1 and B1."
      Laine B., Sautiere P., Spassky A., Rimsky S.
      Biochem. Biophys. Res. Commun. 119:1147-1153(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
    12. "An Escherichia coli protein that preferentially binds to sharply curved DNA."
      Yamada H., Muramatsu S., Mizuno T.
      J. Biochem. 108:420-425(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20.
    13. "Small genes/gene-products in Escherichia coli K-12."
      Wasinger V.C., Humphery-Smith I.
      FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20.
      Strain: K12.
    14. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    15. Cited for: PROTEIN SEQUENCE OF 2-12.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    16. Cited for: PROTEIN SEQUENCE OF 2-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    17. "Expression of the gene encoding the major bacterial nucleotide protein H-NS is subject to transcriptional auto-repression."
      Falconi M., Higgins P.N., Spurio R., Pon C.L., Gualerzi C.O.
      Mol. Microbiol. 10:273-282(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    19. "Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli."
      Ko M., Park C.
      J. Mol. Biol. 303:371-382(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FLAGELLA BIOGENESIS AND MOTILITY, DISRUPTION PHENOTYPE.
      Strain: K12.
    20. "Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli."
      Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R.
      Mol. Microbiol. 62:1014-1034(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN CURLI FIMBRIAE EXPRESSION, DISRUPTION PHENOTYPE.
      Strain: K12 / MC4100.
    21. "Identification and characterization of E. coli CRISPR-cas promoters and their silencing by H-NS."
      Pul U., Wurm R., Arslan Z., Geissen R., Hofmann N., Wagner R.
      Mol. Microbiol. 75:1495-1512(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REPRESSES CRISPR EXPRESSION.
      Strain: K12.
    22. "H-NS-mediated repression of CRISPR-based immunity in Escherichia coli K12 can be relieved by the transcription activator LeuO."
      Westra E.R., Pul U., Heidrich N., Jore M.M., Lundgren M., Stratmann T., Wurm R., Raine A., Mescher M., Van Heereveld L., Mastop M., Wagner E.G., Schnetz K., Van Der Oost J., Wagner R., Brouns S.J.
      Mol. Microbiol. 77:1380-1393(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANTAGONIZED BY LEUO, ROLE IN CRISPR EXPRESSION, DISRUPTION PHENOTYPE.
      Strain: K12.
    23. "Essential residues in the H-NS binding site of Hha, a co-regulator of horizontally acquired genes in Enterobacteria."
      de Alba C.F., Solorzano C., Paytubi S., Madrid C., Juarez A., Garcia J., Pons M.
      FEBS Lett. 585:1765-1770(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHA, MUTAGENESIS OF ARG-12.
      Strain: K12 / MG1655 / ATCC 47076.
    24. "Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli."
      Shindo H., Iwaki T., Ieda R., Kurumizaka H., Ueguchi C., Mizuno T., Morikawa S., Nakamura H., Kuboniwa H.
      FEBS Lett. 360:125-131(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 91-137.
    25. "New insights into transcriptional regulation by H-NS."
      Fang F.C., Rimsky S.
      Curr. Opin. Microbiol. 11:113-120(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiHNS_ECOLI
    AccessioniPrimary (citable) accession number: P0ACF8
    Secondary accession number(s): P08936
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3