DNA-binding protein H-NS - Escherichia coli (strain K12)

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P0ACF8 (HNS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA-binding protein H-NS

Alternative name(s):
Histone-like protein HLP-II
Protein B1
Protein H1

Gene names

Name:	hns
Synonyms:	bglY, cur, drdX, hnsA, msyA, osmZ, pilG, topS
Ordered Locus Names:	b1237, JW1225

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	137 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.17 Ref.19 Ref.20 Ref.22
Subunit structure	Homodimer, it can multimerize into higher-order complexes that form bridges between adjacent DNA helices. Can form a complex with YdgT.
Disruption phenotype	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. Ref.19 Ref.20 Ref.22
Sequence similarities	Belongs to the histone-like protein H-NS family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Ligand	DNA-binding
Molecular function	Repressor
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	bent DNA binding Inferred from direct assay PubMed 10551881. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Chain

2 – 137

136

DNA-binding protein H-NS

PRO_0000168503

Secondary structure

137

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ACF8 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E628184AC7C86F49
Show »

FASTA

137

15,540

        10         20         30         40         50         60 
MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE VEERTRKLQQ 

        70         80         90        100        110        120 
YREMLIADGI DPNELLNSLA AVKSGTKAKR AQRPAKYSYV DENGETKTWT GQGRTPAVIK 

       130 
KAMDEQGKSL DDFLIKQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[16]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] 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]	"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.
[24]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

S00903.

RefSeq

NP_415753.1. NC_000913.2.
YP_489505.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HNR	NMR	-	A	91-137	[»]
1HNS	NMR	-	A	91-137	[»]
1LR1	NMR	-	A/B	2-57	[»]
1NI8	NMR	-	A/B	2-46	[»]

ProteinModelPortal

P0ACF8.

SMR

P0ACF8. Positions 2-81, 91-137.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35853N.

IntAct

P0ACF8. 48 interactions.

MINT

MINT-1223907.

STRING

511145.b1237.

2D gel databases

SWISS-2DPAGE

P0ACF8.

Proteomic databases

PaxDb

P0ACF8.

PRIDE

P0ACF8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74319; AAC74319; b1237.
BAA36117; BAA36117; BAA36117.

GeneID

12934502.
945829.

KEGG

ecj:Y75_p1210.
eco:b1237.

PATRIC

32117730. VBIEscCol129921_1285.

Organism-specific databases

EchoBASE

EB0452.

EcoGene

EG10457. hns.

Phylogenomic databases

eggNOG

COG2916.

HOGENOM

HOG000218473.

K03746.

OMA

PAKYQYV.

ProtClustDB

PRK10947.

Enzyme and pathway databases

BioCyc

EcoCyc:PD00288.
ECOL316407:JW1225-MONOMER.

Gene expression databases

Genevestigator

P0ACF8.

Family and domain databases

InterPro

IPR001801. Histone_HNS.
[Graphical view]

Pfam

PF00816. Histone_HNS. 1 hit.
[Graphical view]

PIRSF

PIRSF002096. HnS. 1 hit.

SMART

SM00528. HNS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ACF8.

Entry information

Entry name

HNS_ECOLI

Accession

Primary (citable) accession number: P0ACF8
Secondary accession number(s): P08936

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents