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P0ACF8

- HNS_ECOLI

UniProt

P0ACF8 - HNS_ECOLI

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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

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

GO - Biological processi

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

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
Complete GO annotation...

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

        10         20         30         40         50
MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE
60 70 80 90 100
VEERTRKLQQ YREMLIADGI DPNELLNSLA AVKSGTKAKR AQRPAKYSYV
110 120 130
DENGETKTWT GQGRTPAVIK KAMDEQGKSL DDFLIKQ
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

« Hide 'large scale' publications
  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 29, 2014
This is version 86 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