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UniProtKB - P0ACF8 (HNS_ECOLI)

Entry version 118 (13 Feb 2019)
Sequence version 2 (23 Jan 2007)
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Protein

DNA-binding protein H-NS

Gene

hns

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

A DNA-binding protein implicated in transcriptional repression (silencing) (PubMed:333393, PubMed:2128918, PubMed:8890170, PubMed:8913298, PubMed:9398522, PubMed:16963779, PubMed:17046956, PubMed:23543115). Also involved in bacterial chromosome organization and compaction (PubMed:6379600, PubMed:10982869, PubMed:21903814). H-NS binds tightly to AT-rich dsDNA and inhibits transcription (PubMed:2512122, PubMed:16963779, PubMed:17435766, PubMed:17881364, PubMed:23543115). Binds upstream and downstream of initiating RNA polymerase, trapping it in a loop and preventing transcription (PubMed:11714691). Binds to hundreds of sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome (PubMed:16963779, PubMed:17046956, PubMed:23543115). Many of these loci were horizontally transferred (HTG); this offers the selective advantage of silencing foreign DNA while keeping it in the genome in case of need (PubMed:17046956, PubMed:17881364, PubMed:26789284). Suppresses transcription at many intragenic sites as well as transcription of spurious, non-coding RNAs genome-wide (PubMed:24449106). Repression of HTG by H-NS is thought to allow their DNA to evolve faster than non-H-NS-bound regions, and facilitates integration of HTG into transcriptional regulatory networks (PubMed:26789284). A subset of H-NS/StpA-regulated genes also require Hha (and/or Cnu, ydgT) for repression; Hha and Cnu increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex (PubMed:23543115). The protein forms 2 clusters in the nucleoid which gather hns-bound loci together, bridging non-contiguous DNA, and causes DNA substantial condensation (PubMed:21903814). Binds DNA better at low temperatures than at 37 degrees Celsius; AT-rich sites nucleate H-NS binding, further DNA-binding is cooperative and this cooperativity decreases with rising temperature (PubMed:17435766, PubMed:17881364). Transcriptional repression can be inhibited by dominant-negative mutants of StpA or itself (PubMed:8755860). May effect transcriptional elongation (PubMed:25638302). Can increase translational efficiency of mRNA with suboptimal Shine-Dalgarno sequences (PubMed:20595230). Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD (PubMed:17010156). Plays a role in flagellar function (PubMed:11031114). Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its repression is antagonized by LeuO (PubMed:20132443, PubMed:20659289). Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150 (PubMed:7934818). Overexpression suppresses secY24, a temperature-sensitive mutation (PubMed:1537791). Has also been reported to activate transcription of some genes (PubMed:4566454, PubMed:338303, PubMed:2128918).1 Publication27 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei12Interacts with Hha1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi112 – 117By similarity6

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Repressor, RNA-binding
Biological processStress response, Transcription, Transcription regulation, Translation regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:PD00288
ECOL316407:JW1225-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-binding protein H-NS1 Publication
Alternative name(s):
Heat-stable nucleoid-structuring protein1 Publication
Histone-like protein HLP-II
Protein B11 Publication
Protein H11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:hns1 Publication
Synonyms:bglY1 Publication, cur, drdX1 Publication, hnsA, msyA1 Publication, osmZ1 Publication, pilG, topS
Ordered Locus Names:b1237, JW1225
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10457 hns

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Decreased growth below 30 degrees Celsius (PubMed:1691451). Altered expression of a number of genes (PubMed:2128918, PubMed:8890170, PubMed:8913298, PubMed:23543115). Derepression of the cryptic blg operon (PubMed:8913298, PubMed:11790731). Alteration of chromosome organization (PubMed:21903814). Double hns-stpA mutants grow slower and have reduced viable cell counts compared to single hns mutants in MC1029 and MC4100 backgrounds (PubMed:8890170). In 0.3M NaCl a double hns-stpA deletion up-regulates 583 and down-regulates 86 genes, 363 of which are thought to have been horizontally acquired; 131 are also up-regulated in a double cnu-hha deletion (PubMed:23543115). At 28 degrees Celsius csgD transcription is reduced (PubMed:17010156). Flagella loss due to reduced expression of the flhDC operon (PubMed:11031114). Flagella can be restored by expression of flhDC, but strains are non-motile, suggesting H-NS also plays a role in flagellar function (PubMed:11031114). Disruption leads to increased expression of CRISPR-cas genes and increased viral resistance (PubMed:20659289).10 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2 – 69Missing : No longer complements a deletion mutant, has no dominant-negative effects on wild-type protein, does not oligomerize. 1 PublicationAdd BLAST68
Mutagenesisi2 – 20Missing : No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes. 1 PublicationAdd BLAST19
Mutagenesisi6K → P: No effect on oligomerization of N-terminal fragment 1-89. 1 Publication1
Mutagenesisi12 – 15RTLR → ERLA: Decreased DNA-binding, loss of preference for curved DNA. 1 Publication4
Mutagenesisi12R → C: Derepression of proV and bgl expression, normal DNA-binding, normal oligomerization. 1 Publication1
Mutagenesisi12R → H: Derepression of proV and bgl expression, normal DNA-binding, normal oligomerization. Fragments 1-46 and 1-64 no longer bind Hha. 2 Publications1
Mutagenesisi12R → K: Abolishes the interaction with Hha. 1 Publication1
Mutagenesisi15R → C: Derepression of proV and bgl expression. 1 Publication1
Mutagenesisi15R → H: Derepression of proV and bgl expression. Fragments 1-46 and 1-64 fold incorrectly but still bind Hha. 2 Publications1
Mutagenesisi17Q → P: Abolishes oligomerization of N-terminal fragment 1-89. 1 Publication1
Mutagenesisi26L → P: Partial loss of repressor function. 1 Publication1
Mutagenesisi30L → A or K: Wild-type function. 1 Publication1
Mutagenesisi30L → D: Derepression of proV and partial derepression of bgl epxression, does not dimerize, anomalous protein mobility on gels. 1 Publication1
Mutagenesisi30L → P: Derepression of proV and bgl epxression, does not dimerize, anomalous protein mobility on gels. Protein localizes to nucleoid but no longer forms discreet compact clusters. 2 Publications1
Mutagenesisi32K → Q: Loss of Hha binding by fragment 1-64, protein folding is unaffected. 1 Publication1
Mutagenesisi53 – 55ERT → GRP: Partial loss of repressor function. 1 Publication3
Mutagenesisi54R → C: Derepression of proV and bgl expression. 1 Publication1
Mutagenesisi64 – 137Missing : No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes. 2 PublicationsAdd BLAST74
Mutagenesisi90R → C or H: Derepression of proV expression. 1 Publication1
Mutagenesisi91A → T: Derepression of proV expression. 1 Publication1
Mutagenesisi92 – 137Missing : Derepression of proV expression, loss of DNA-binding, increased oligomerization. No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes. 2 PublicationsAdd BLAST46
Mutagenesisi93R → C: Derepression of proV expression. 1 Publication1
Mutagenesisi94P → L or S: Derepression of proV expression. 1 Publication1
Mutagenesisi95A → T: Derepression of proV expression. 1 Publication1
Mutagenesisi97Y → C, H or S: Partial loss of repressor function. 1 Publication1
Mutagenesisi110T → A: Partial loss of repressor function. 1 Publication1
Mutagenesisi110T → I: Derepression of proV expression. 1 Publication1
Mutagenesisi111G → D or S: Derepression of proV expression. 1 Publication1
Mutagenesisi113G → D: Derepression of proV expression, decreased DNA-binding but still prefers curved DNA, increased oligomerization. 1 Publication1
Mutagenesisi113G → S: Partial loss of repressor function. 1 Publication1
Mutagenesisi114R → C or H: Derepression of proV expression. 1 Publication1
Mutagenesisi115T → I: Derepression of proV expression. 1 Publication1
Mutagenesisi116P → S: Partial loss of repressor function. Protein localizes to nucleoid but forms about 20-fold fewer localization points. 2 Publications1
Mutagenesisi119I → T: Partial loss of repressor function. 1 Publication1
Mutagenesisi122 – 137AMDEQ…FLIKQ → KQWMRKVNPSTIS: Partial loss of repressor function. 1 PublicationAdd BLAST16
Mutagenesisi133F → S: Partial loss of repressor function. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved9 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001685032 – 137DNA-binding protein H-NSAdd BLAST136

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Cells (strain MRE-600) in mid-exponential phase have three 15.5 kDa proteins with 3 different isoelectric points; the major form (H1a, pI 7.5) rises in concentration during growth while the 2 minor forms (H1b, pI about 7.2 and H1c, pI 7.0) remain approximately constant (PubMed:6379600).1 Publication

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0ACF8

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0ACF8

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P0ACF8

PRoteomics IDEntifications database

More...PRIDEi		P0ACF8

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0ACF8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Protein levels rise from about 4,000/cell in exponential phase to about 18,000/cell in late stationary phase (at protein level) (PubMed:6379600). Subject to transcriptional auto-repression (PubMed:7934818). Induced by increased hydrostatic pressure (PubMed:8226663). hns transcription can be repressed by overexpressed StpA (which is usually repressed by hns) (PubMed:8890170). Induced by cold shock (42 to 15 degrees Celsius) (at protein level) (PubMed:8898389).5 Publications

Gene expression databases

CollecTF database of bacterial transcription factor binding sites

More...CollecTFi		EXPREG_00000830

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer, also found as tetramers or higher oligomers (PubMed:4566454, PubMed:338303, PubMed:3135462, PubMed:8913298, PubMed:9398522, PubMed:8755860, PubMed:12460581, PubMed:23601147). Oligomerizes into higher-order complexes that form bridges between adjacent DNA helices. The N-terminal region (residues 1-64) can interact with overexpressed StpA (PubMed:8755860). Forms a complex with Cnu (YdgT) (PubMed:21600204). The H-NS dimer forms a heterotrimeric complex with Hha in the absence of DNA; this is mediated by residues 1-46 (PubMed:21600204, PubMed:11790731, PubMed:16650431, PubMed:26085102). Interacts with Hfq (PubMed:2020545).1 Publication12 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4263496, 155 interactors
850196, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1965 H-NS complex, dimeric
CPX-1966 H-NS complex, tetrameric
CPX-1979 H-NS-Hha transcription factor complex
CPX-1980 H-NS-Cnu transcription factor complex

Database of interacting proteins

More...DIPi		DIP-35853N

Protein interaction database and analysis system

More...IntActi		P0ACF8, 54 interactors

Molecular INTeraction database

More...MINTi		P0ACF8

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_1297

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1137
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HNRNMR-A91-137[»]
1HNSNMR-A91-137[»]
1LR1NMR-A/B2-58[»]
1NI8NMR-A/B2-47[»]
2MW2NMR-B/C1-47[»]

Database of protein disorder

More...DisProti		DP00776

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P0ACF8

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0ACF8

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0ACF8

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni21 – 63Involved in dimerization1 PublicationAdd BLAST43
Regioni92 – 137Required for DNA-binding1 PublicationAdd BLAST46

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili22 – 492 PublicationsAdd BLAST28

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

A central region (about residues 21-47) is involved in dimerization, but multimerization requires other residues (PubMed:8755860, PubMed:9398522, PubMed:16650431, PubMed:12460581, PubMed:12592399). The dimerization domain (1-47) also acts as a hinge; changes in its structure probably impact oligomerization and DNA-binding geometries (PubMed:23601147). The N-terminus also interacts with Hha, perhaps via residues 2-18; a well-folded dimer is not necessary for Hha binding (PubMed:16650431). The C-terminus (residues 92-137) binds DNA (PubMed:8913298). Residues in the N-terminus contribute to DNA-binding and to discrimination between curved and non-curved DNA (PubMed:12592399).7 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4108SAU Bacteria
COG2916 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000218473

KEGG Orthology (KO)

More...KOi		K03746

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.287.1050, 1 hit
4.10.430.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027444 H-NS_C_dom
IPR037150 H-NS_C_dom_sf
IPR001801 Histone_HNS
IPR027454 Histone_HNS_N

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00816 Histone_HNS, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002096 HnS, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00528 HNS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE628184AC7C86F49
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 15407.8 Da from positions 2 - 137. Determined by MALDI. A second experiment gave a mass of 15410.1.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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
Y00976 Genomic DNA Translation: CAA68786.1
U00096 Genomic DNA Translation: AAC74319.1
AP009048 Genomic DNA Translation: BAA36117.1

Protein sequence database of the Protein Information Resource

More...PIRi		S00903

NCBI Reference Sequences

More...RefSeqi		NP_415753.1, NC_000913.3
WP_001287378.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74319; AAC74319; b1237
BAA36117; BAA36117; BAA36117

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945829

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1225
eco:b1237

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1048

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
Y00976 Genomic DNA Translation: CAA68786.1
U00096 Genomic DNA Translation: AAC74319.1
AP009048 Genomic DNA Translation: BAA36117.1
PIRiS00903
RefSeqiNP_415753.1, NC_000913.3
WP_001287378.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HNRNMR-A91-137[»]
1HNSNMR-A91-137[»]
1LR1NMR-A/B2-58[»]
1NI8NMR-A/B2-47[»]
2MW2NMR-B/C1-47[»]
DisProtiDP00776
ProteinModelPortaliP0ACF8
SMRiP0ACF8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263496, 155 interactors
850196, 1 interactor
ComplexPortaliCPX-1965 H-NS complex, dimeric
CPX-1966 H-NS complex, tetrameric
CPX-1979 H-NS-Hha transcription factor complex
CPX-1980 H-NS-Cnu transcription factor complex
DIPiDIP-35853N
IntActiP0ACF8, 54 interactors
MINTiP0ACF8
STRINGi316385.ECDH10B_1297

2D gel databases

SWISS-2DPAGEiP0ACF8

Proteomic databases

EPDiP0ACF8
jPOSTiP0ACF8
PaxDbiP0ACF8
PRIDEiP0ACF8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74319; AAC74319; b1237
BAA36117; BAA36117; BAA36117
GeneIDi945829
KEGGiecj:JW1225
eco:b1237
PATRICifig|1411691.4.peg.1048

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0452
EcoGeneiEG10457 hns

Phylogenomic databases

eggNOGiENOG4108SAU Bacteria
COG2916 LUCA
HOGENOMiHOG000218473
KOiK03746

Enzyme and pathway databases

BioCyciEcoCyc:PD00288
ECOL316407:JW1225-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0ACF8

Protein Ontology

More...PROi		PR:P0ACF8

Gene expression databases

CollecTFiEXPREG_00000830

Family and domain databases

Gene3Di1.10.287.1050, 1 hit
4.10.430.10, 1 hit
InterProiView protein in InterPro
IPR027444 H-NS_C_dom
IPR037150 H-NS_C_dom_sf
IPR001801 Histone_HNS
IPR027454 Histone_HNS_N
PfamiView protein in Pfam
PF00816 Histone_HNS, 1 hit
PIRSFiPIRSF002096 HnS, 1 hit
SMARTiView protein in SMART
SM00528 HNS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHNS_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0ACF8
Secondary accession number(s): P08936, Q47267
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 118 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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