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ECOLI:HNS

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) hns (synonyms: bglY, cur, drdX, hnsA, msyA, osmZ, pilG, topS)
Protein Name(s) DNA-binding protein H-NS

Histone-like protein HLP-II Protein B1 Protein H1

External Links
UniProt P0ACF8
EMBL X07688
X59940
X57231
X67326
U00096
AP009048
PIR S00903
RefSeq NP_415753.1
YP_489505.1
PDB 1HNR
1HNS
1LR1
1NI8
PDBsum 1HNR
1HNS
1LR1
1NI8
ProteinModelPortal P0ACF8
SMR P0ACF8
BioGrid 850196
DIP DIP-35853N
IntAct P0ACF8
MINT MINT-1223907
STRING 511145.b1237
SWISS-2DPAGE P0ACF8
PaxDb P0ACF8
PRIDE P0ACF8
EnsemblBacteria AAC74319
BAA36117
GeneID 12934502
945829
KEGG ecj:Y75_p1210
eco:b1237
PATRIC 32117730
EchoBASE EB0452
EcoGene EG10457
eggNOG COG2916
HOGENOM HOG000218473
KO K03746
OMA LQQYRDM
OrthoDB EOG6NPM97
BioCyc EcoCyc:PD00288
ECOL316407:JW1225-MONOMER
EvolutionaryTrace P0ACF8
PRO PR:P0ACF8
Proteomes UP000000318
UP000000625
Genevestigator P0ACF8
GO GO:0005622
GO:0016020
GO:0003681
GO:0042802
GO:0006355
GO:0006351
Gene3D 1.10.287.1050
4.10.430.10
InterPro IPR027444
IPR001801
IPR027454
Pfam PF00816
PIRSF PIRSF002096
SMART SM00528

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016481

negative regulation of transcription

PMID:16385041[1]

ECO:0000314

P

See Fig 3. The preferential binding to the Py region shows that H-NS down-regulates transcription from Py

complete

GO:0045943

positive regulation of transcription from RNA polymerase I promoter

PMID:10801345[2]

ECO:0000314

P

See Fig 5

complete

GO:0016072

negative regulation of rRNA processing

PMID:9632265[3]

ECO:0000315

P

see Fig 1 and Fig 2

complete

part_of

GO:0016020

membrane

PMID:16858726[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0045892

negative regulation of transcription, DNA-templated

PMID:21708124[5]

ECO:0001808

reverse transcription polymerase chain reaction evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045892

negative regulation of transcription, DNA-templated

PMID:20015147[6]

ECO:0001204

in vitro transcription assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045892

negative regulation of transcription, DNA-templated

PMID:20015147[6]

ECO:0000279

western blot evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:21708124[5]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.3

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:20015147[6]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.3

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:21778209[7]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:21708124[5]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:20015147[6]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:21708124[5]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.3

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:20015147[6]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.3

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:21778209[7]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:21708124[5]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:20015147[6]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:21708124[5]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.3

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:20015147[6]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_000913.3

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:21778209[7]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:21708124[5]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:20015147[6]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10457
PANTHER:PTN002211313
UniProtKB:Q9KSX6

C

Seeded From UniProt

complete

involved_in

GO:0016458

gene silencing

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002211313
UniProtKB:P0A1S2

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10457
EcoGene:EG11554
PANTHER:PTN002211313

C

Seeded From UniProt

complete

enables

GO:0003681

bent DNA binding

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10457
PANTHER:PTN002211313
UniProtKB:P0A1S2

F

Seeded From UniProt

complete

enables

GO:0003680

AT DNA binding

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002211313
UniProtKB:P0A1S2

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11554
PANTHER:PTN002211313

F

Seeded From UniProt

complete

enables

GO:0001217

DNA-binding transcription repressor activity

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10457
PANTHER:PTN002211313
UniProtKB:Q9KSX6

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10457
PANTHER:PTN002211313
UniProtKB:Q9KSX6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:9398522[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ACF8

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16303134[10]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ACF8

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:12592399[11]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ACF8

F

Seeded From UniProt

complete

enables

GO:0003681

bent DNA binding

PMID:10551881[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:1900232

negative regulation of single-species biofilm formation on inanimate substrate

PMID:28470798[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[15]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001801
InterPro:IPR027444
InterPro:IPR037150

F

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001801

P

Seeded From UniProt

complete

enables

GO:0046983

protein dimerization activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR027454

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

involved_in

GO:0006417

regulation of translation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0810

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

part_of

GO:0009295

nucleoid

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0187

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Will, WR & Frost, LS (2006) Characterization of the opposing roles of H-NS and TraJ in transcriptional regulation of the F-plasmid tra operon. J. Bacteriol. 188 507-14 PubMed GONUTS page
  2. Schröder, O & Wagner, R (2000) The bacterial DNA-binding protein H-NS represses ribosomal RNA transcription by trapping RNA polymerase in the initiation complex. J. Mol. Biol. 298 737-48 PubMed GONUTS page
  3. Afflerbach, H et al. (1998) Effects of the Escherichia coli DNA-binding protein H-NS on rRNA synthesis in vivo. Mol. Microbiol. 28 641-53 PubMed GONUTS page
  4. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 5.4 5.5 5.6 Moreira, RN et al. (2011) A new target for an old regulator: H-NS represses transcription of bolA morphogene by direct binding to both promoters. Biochem. Biophys. Res. Commun. 411 50-5 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 6.5 6.6 6.7 Nandal, A et al. (2010) Induction of the ferritin gene (ftnA) of Escherichia coli by Fe(2+)-Fur is mediated by reversal of H-NS silencing and is RyhB independent. Mol. Microbiol. 75 637-57 PubMed GONUTS page
  7. 7.0 7.1 7.2 Cagle, CA et al. (2011) Regulation of the integrase and cassette promoters of the class 1 integron by nucleoid-associated proteins. Microbiology (Reading, Engl.) 157 2841-53 PubMed GONUTS page
  8. 8.0 8.1 8.2 8.3 8.4 8.5 8.6 8.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  9. Ueguchi, C et al. (1997) Clarification of the dimerization domain and its functional significance for the Escherichia coli nucleoid protein H-NS. J. Mol. Biol. 274 145-51 PubMed GONUTS page
  10. Stella, S et al. (2006) Environmental control of the in vivo oligomerization of nucleoid protein H-NS. J. Mol. Biol. 355 169-74 PubMed GONUTS page
  11. Bloch, V et al. (2003) The H-NS dimerization domain defines a new fold contributing to DNA recognition. Nat. Struct. Biol. 10 212-8 PubMed GONUTS page
  12. Azam, TA & Ishihama, A (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J. Biol. Chem. 274 33105-13 PubMed GONUTS page
  13. Parker, A et al. (2017) Alternative pathways for Escherichia coli biofilm formation revealed by sRNA overproduction. Mol. Microbiol. 105 309-325 PubMed GONUTS page
  14. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  15. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page