ECOLI:HNS

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	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
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Notes

References

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

↑ 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
↑ 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
↑ 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
↑ 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
↑ ^5.0 ^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
↑ ^6.0 ^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
↑ ^7.0 ^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
↑ ^8.0 ^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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Parker, A et al. (2017) Alternative pathways for Escherichia coli biofilm formation revealed by sRNA overproduction. Mol. Microbiol. 105 309-325 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ 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

[PMID:16385041-1] 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

[PMID:10801345-2] 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

[PMID:9632265-3] 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

[PMID:16858726-4] 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

[PMID:21708124-5] 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

[PMID:20015147-6] 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

[PMID:21778209-7] 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

[PMID:21873635-8] 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

[PMID:9398522-9] 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

[PMID:16303134-10] 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

[PMID:12592399-11] 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

[PMID:10551881-12] 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

[PMID:28470798-13] Parker, A et al. (2017) Alternative pathways for Escherichia coli biofilm formation revealed by sRNA overproduction. Mol. Microbiol. 105 309-325 PubMed GONUTS page

[PMID:18304323-14] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-15] 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

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ECOLI:HNS

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