UniProtKB - P0ACF8 (HNS_ECOLI)
DNA-binding protein H-NS
hns
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 12 | Interacts with Hha1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 112 – 117 | By similarity | 6 |
GO - Molecular functioni
- bent DNA binding Source: EcoliWiki
- DNA binding Source: GO_Central
- DNA-binding transcription repressor activity Source: CollecTF
- identical protein binding Source: IntAct
- minor groove of adenine-thymine-rich DNA binding Source: GO_Central
- protein dimerization activity Source: InterPro
- RNA binding Source: UniProtKB-KW
- transcription regulatory region sequence-specific DNA binding Source: CollecTF
GO - Biological processi
- gene silencing Source: GO_Central
- negative regulation of single-species biofilm formation on inanimate substrate Source: EcoCyc
- negative regulation of transcription, DNA-templated Source: CollecTF
- regulation of translation Source: UniProtKB-KW
Keywordsi
Molecular function | DNA-binding, Repressor, RNA-binding |
Biological process | Stress response, Transcription, Transcription regulation, Translation regulation |
Enzyme and pathway databases
BioCyci | EcoCyc:PD00288 |
Names & Taxonomyi
Protein namesi | Recommended name: DNA-binding protein H-NS1 PublicationAlternative name(s): Heat-stable nucleoid-structuring protein1 Publication Histone-like protein HLP-II Protein B11 Publication Protein H11 Publication |
Gene namesi | Name:hns1 Publication Synonyms:bglY1 Publication, cur, drdX1 Publication, hnsA, msyA1 Publication, osmZ1 Publication, pilG, topS Ordered Locus Names:b1237, JW1225 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- nucleoid 2 Publications Note: Forms 2 compact clusters per chromosome, located at one-quarter and three-quarter positions on the cell's long axis: 2 H-NS-repressed genes were closely associated with H-NS clusters while a non-H-NS-repressed gene was not substantially associated with the H-NS cluster (PubMed:21903814).1 Publication
GO - Cellular componenti
- cytosol Source: EcoCyc
- membrane Source: UniProtKB
- nucleoid Source: UniProtKB-SubCell
- protein-DNA complex Source: CollecTF
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 – 69 | Missing : No longer complements a deletion mutant, has no dominant-negative effects on wild-type protein, does not oligomerize. 1 PublicationAdd BLAST | 68 | |
Mutagenesisi | 2 – 20 | Missing : No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes. 1 PublicationAdd BLAST | 19 | |
Mutagenesisi | 6 | K → P: No effect on oligomerization of N-terminal fragment 1-89. 1 Publication | 1 | |
Mutagenesisi | 12 – 15 | RTLR → ERLA: Decreased DNA-binding, loss of preference for curved DNA. 1 Publication | 4 | |
Mutagenesisi | 12 | R → C: Derepression of proV and bgl expression, normal DNA-binding, normal oligomerization. 1 Publication | 1 | |
Mutagenesisi | 12 | R → H: Derepression of proV and bgl expression, normal DNA-binding, normal oligomerization. Fragments 1-46 and 1-64 no longer bind Hha. 2 Publications | 1 | |
Mutagenesisi | 12 | R → K: Abolishes the interaction with Hha. 1 Publication | 1 | |
Mutagenesisi | 15 | R → C: Derepression of proV and bgl expression. 1 Publication | 1 | |
Mutagenesisi | 15 | R → H: Derepression of proV and bgl expression. Fragments 1-46 and 1-64 fold incorrectly but still bind Hha. 2 Publications | 1 | |
Mutagenesisi | 17 | Q → P: Abolishes oligomerization of N-terminal fragment 1-89. 1 Publication | 1 | |
Mutagenesisi | 26 | L → P: Partial loss of repressor function. 1 Publication | 1 | |
Mutagenesisi | 30 | L → A or K: Wild-type function. 1 Publication | 1 | |
Mutagenesisi | 30 | L → D: Derepression of proV and partial derepression of bgl epxression, does not dimerize, anomalous protein mobility on gels. 1 Publication | 1 | |
Mutagenesisi | 30 | L → 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 Publications | 1 | |
Mutagenesisi | 32 | K → Q: Loss of Hha binding by fragment 1-64, protein folding is unaffected. 1 Publication | 1 | |
Mutagenesisi | 53 – 55 | ERT → GRP: Partial loss of repressor function. 1 Publication | 3 | |
Mutagenesisi | 54 | R → C: Derepression of proV and bgl expression. 1 Publication | 1 | |
Mutagenesisi | 64 – 137 | Missing : No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes. 2 PublicationsAdd BLAST | 74 | |
Mutagenesisi | 90 | R → C or H: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 91 | A → T: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 92 – 137 | Missing : 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 BLAST | 46 | |
Mutagenesisi | 93 | R → C: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 94 | P → L or S: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 95 | A → T: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 97 | Y → C, H or S: Partial loss of repressor function. 1 Publication | 1 | |
Mutagenesisi | 110 | T → A: Partial loss of repressor function. 1 Publication | 1 | |
Mutagenesisi | 110 | T → I: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 111 | G → D or S: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 113 | G → D: Derepression of proV expression, decreased DNA-binding but still prefers curved DNA, increased oligomerization. 1 Publication | 1 | |
Mutagenesisi | 113 | G → S: Partial loss of repressor function. 1 Publication | 1 | |
Mutagenesisi | 114 | R → C or H: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 115 | T → I: Derepression of proV expression. 1 Publication | 1 | |
Mutagenesisi | 116 | P → S: Partial loss of repressor function. Protein localizes to nucleoid but forms about 20-fold fewer localization points. 2 Publications | 1 | |
Mutagenesisi | 119 | I → T: Partial loss of repressor function. 1 Publication | 1 | |
Mutagenesisi | 122 – 137 | AMDEQ…FLIKQ → KQWMRKVNPSTIS: Partial loss of repressor function. 1 PublicationAdd BLAST | 16 | |
Mutagenesisi | 133 | F → S: Partial loss of repressor function. 1 Publication | 1 |
Miscellaneous databases
PHI-basei | PHI:6369 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed9 Publications | |||
ChainiPRO_0000168503 | 2 – 137 | DNA-binding protein H-NSAdd BLAST | 136 |
Post-translational modificationi
Proteomic databases
jPOSTi | P0ACF8 |
PaxDbi | P0ACF8 |
PRIDEi | P0ACF8 |
2D gel databases
SWISS-2DPAGEi | P0ACF8 |
Expressioni
Inductioni
Gene expression databases
CollecTFi | EXPREG_00000830 |
Interactioni
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 PublicationsBinary interactionsi
Hide detailsP0ACF8
With | #Exp. | IntAct |
---|---|---|
cnu [P64467] | 3 | EBI-544934,EBI-551907 |
hha [P0ACE3] | 5 | EBI-544934,EBI-1122578 |
itself | 10 | EBI-544934,EBI-544934 |
stpA [P0ACG1] | 4 | EBI-544934,EBI-551928 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- protein dimerization activity Source: InterPro
Protein-protein interaction databases
BioGRIDi | 4263496, 155 interactors 850196, 2 interactors |
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 |
DIPi | DIP-35853N |
IntActi | P0ACF8, 54 interactors |
MINTi | P0ACF8 |
STRINGi | 511145.b1237 |
Structurei
Secondary structure
3D structure databases
BMRBi | P0ACF8 |
SMRi | P0ACF8 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0ACF8 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 21 – 63 | Involved in dimerization1 PublicationAdd BLAST | 43 | |
Regioni | 92 – 137 | Required for DNA-binding1 PublicationAdd BLAST | 46 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 22 – 49 | 2 PublicationsAdd BLAST | 28 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Coiled coilPhylogenomic databases
eggNOGi | COG2916, Bacteria |
HOGENOMi | CLU_117503_0_0_6 |
Family and domain databases
DisProti | DP00776 |
Gene3Di | 1.10.287.1050, 1 hit 4.10.430.10, 1 hit |
InterProi | View protein in InterPro IPR027444, H-NS_C_dom IPR037150, H-NS_C_dom_sf IPR001801, Histone_HNS IPR027454, Histone_HNS_N |
Pfami | View protein in Pfam PF00816, Histone_HNS, 1 hit |
PIRSFi | PIRSF002096, HnS, 1 hit |
SMARTi | View protein in SMART SM00528, HNS, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Mass spectrometryi
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 |
PIRi | S00903 |
RefSeqi | NP_415753.1, NC_000913.3 WP_001287378.1, NZ_STEB01000005.1 |
Genome annotation databases
EnsemblBacteriai | AAC74319; AAC74319; b1237 BAA36117; BAA36117; BAA36117 |
GeneIDi | 49584978 945829 |
KEGGi | ecj:JW1225 eco:b1237 |
PATRICi | fig|1411691.4.peg.1048 |
Similar proteinsi
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 |
PIRi | S00903 |
RefSeqi | NP_415753.1, NC_000913.3 WP_001287378.1, NZ_STEB01000005.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
2MW2 | NMR | - | B/C | 1-47 | [»] | |
BMRBi | P0ACF8 | |||||
SMRi | P0ACF8 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263496, 155 interactors 850196, 2 interactors |
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 |
DIPi | DIP-35853N |
IntActi | P0ACF8, 54 interactors |
MINTi | P0ACF8 |
STRINGi | 511145.b1237 |
2D gel databases
SWISS-2DPAGEi | P0ACF8 |
Proteomic databases
jPOSTi | P0ACF8 |
PaxDbi | P0ACF8 |
PRIDEi | P0ACF8 |
Genome annotation databases
EnsemblBacteriai | AAC74319; AAC74319; b1237 BAA36117; BAA36117; BAA36117 |
GeneIDi | 49584978 945829 |
KEGGi | ecj:JW1225 eco:b1237 |
PATRICi | fig|1411691.4.peg.1048 |
Organism-specific databases
EchoBASEi | EB0452 |
Phylogenomic databases
eggNOGi | COG2916, Bacteria |
HOGENOMi | CLU_117503_0_0_6 |
Enzyme and pathway databases
BioCyci | EcoCyc:PD00288 |
Miscellaneous databases
EvolutionaryTracei | P0ACF8 |
PHI-basei | PHI:6369 |
PROi | PR:P0ACF8 |
Gene expression databases
CollecTFi | EXPREG_00000830 |
Family and domain databases
DisProti | DP00776 |
Gene3Di | 1.10.287.1050, 1 hit 4.10.430.10, 1 hit |
InterProi | View protein in InterPro IPR027444, H-NS_C_dom IPR037150, H-NS_C_dom_sf IPR001801, Histone_HNS IPR027454, Histone_HNS_N |
Pfami | View protein in Pfam PF00816, Histone_HNS, 1 hit |
PIRSFi | PIRSF002096, HnS, 1 hit |
SMARTi | View protein in SMART SM00528, HNS, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HNS_ECOLI | |
Accessioni | P0ACF8Primary (citable) accession number: P0ACF8 Secondary accession number(s): P08936, Q47267 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 22, 2005 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 133 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families