{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0ACF8","secondaryAccessions":["P08936","Q47267"],"uniProtkbId":"HNS_ECOLI","entryAudit":{"firstPublicDate":"2005-11-22","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":157,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2841565"}],"value":"DNA-binding protein H-NS"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"6395665"}],"value":"Heat-stable nucleoid-structuring protein"}},{"fullName":{"value":"Histone-like protein HLP-II"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"333393"}],"value":"Protein B1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"4566454"}],"value":"Protein H1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2841565"}],"value":"hns"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2177526"}],"value":"bglY"},{"value":"cur"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1691451"}],"value":"drdX"},{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"h-ns"},{"value":"hnsA"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1537791"}],"value":"msyA"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2177526"}],"value":"osmZ"},{"value":"pilG"},{"value":"topS"}],"orderedLocusNames":[{"value":"b1237"},{"value":"JW1225"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10982869"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11031114"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11714691"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1537791"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16963779"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17010156"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17046956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17435766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17881364"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20132443"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20595230"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20659289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2128918"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21903814"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23543115"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24449106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2512122"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26789284"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"333393"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"338303"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4566454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6379600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7934818"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8755860"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8890170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8913298"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9398522"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25638302"}],"value":"A DNA-binding protein implicated in transcriptional repression (silencing) (PubMed:16963779, PubMed:17046956, PubMed:2128918, PubMed:23543115, PubMed:333393, PubMed:8890170, PubMed:8913298, PubMed:9398522). Also involved in bacterial chromosome organization and compaction (PubMed:10982869, PubMed:21903814, PubMed:6379600). H-NS binds tightly to AT-rich dsDNA and inhibits transcription (PubMed:16963779, PubMed:17435766, PubMed:17881364, PubMed:23543115, PubMed:2512122). 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 affect 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:2128918, PubMed:338303, PubMed:4566454)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34903851"}],"value":"Hydroxyisobutyrylation on Lys-121 (K121hib) decreases the DNA-binding activity of H-NS, promotes the expression of acid-resistance genes and enhances bacterial survival under extreme acid stress"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11790731"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16650431"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2020545"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21600204"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26085102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3135462"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"338303"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4566454"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8755860"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8913298"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9398522"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12460581"}],"value":"Homodimer, also found as tetramers or higher oligomers (PubMed:12460581, PubMed:23601147, PubMed:3135462, PubMed:338303, PubMed:4566454, PubMed:8755860, PubMed:8913298, PubMed:9398522). 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:11790731, PubMed:16650431, PubMed:21600204, PubMed:26085102). Interacts with Hfq (PubMed:2020545)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0ACF8","intActId":"EBI-544934"},"interactantTwo":{"uniProtKBAccession":"P64467","geneName":"cnu","intActId":"EBI-551907"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0ACF8","intActId":"EBI-544934"},"interactantTwo":{"uniProtKBAccession":"P0ACE3","geneName":"hha","intActId":"EBI-1122578"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0ACF8","intActId":"EBI-544934"},"interactantTwo":{"uniProtKBAccession":"P0ACF8","geneName":"hns","intActId":"EBI-544934"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0ACF8","intActId":"EBI-544934"},"interactantTwo":{"uniProtKBAccession":"P0ACG1","geneName":"stpA","intActId":"EBI-551928"},"numberOfExperiments":4,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21903814"}],"value":"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)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21903814"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"333393"}],"value":"Cytoplasm, nucleoid","id":"SL-0187"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6379600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7934818"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8226663"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8890170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8898389"}],"value":"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)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12460581"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12592399"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16650431"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601147"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8755860"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8913298"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9398522"}],"value":"A central region (about residues 21-47) is involved in dimerization, but multimerization requires other residues (PubMed:12460581, PubMed:12592399, PubMed:16650431, PubMed:8755860, PubMed:9398522). 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)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34903851"}],"value":"2-hydroxyisobutyrylated by TmcA on Lys-121"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6379600"}],"value":"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)"}],"commentType":"PTM"},{"commentType":"MASS SPECTROMETRY","method":"MALDI","molWeight":15407.8,"molWeightError":0.0,"note":"A second experiment gave a mass of 15410.1.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11790731"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11031114"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11790731"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1691451"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17010156"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20659289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2128918"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21903814"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23543115"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8890170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8913298"}],"value":"Decreased growth below 30 degrees Celsius (PubMed:1691451). Altered expression of a number of genes (PubMed:2128918, PubMed:23543115, PubMed:8890170, PubMed:8913298). Derepression of the cryptic blg operon (PubMed:11790731, PubMed:8913298). 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)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the histone-like protein H-NS family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11790731"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2020545"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2126011"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6370250"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6395665"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9298646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9600841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9868784"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.16"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"DNA-binding protein H-NS","featureId":"PRO_0000168503"},{"type":"DNA binding","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0A1S2"}]},{"type":"Region","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Involved in dimerization","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9398522"}]},{"type":"Region","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Required for DNA-binding","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8913298"}]},{"type":"Coiled coil","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12460581"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12592399"}]},{"type":"Site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Interacts with Hha","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21600204"}]},{"type":"Modified residue","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34903851"}]},{"type":"Mutagenesis","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"No longer complements a deletion mutant, has no dominant-negative effects on wild-type protein, does not oligomerize.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9398522"}],"alternativeSequence":{}},{"type":"Mutagenesis","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"No longer complements a deletion mutant, has dominant-negative effects on wild-type protein, oligomerizes.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9398522"}],"alternativeSequence":{}},{"type":"Mutagenesis","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"No effect on oligomerization of N-terminal fragment 1-89.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12460581"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["P"]}},{"type":"Mutagenesis","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Decreased DNA-binding, loss of preference for curved DNA.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12592399"}],"alternativeSequence":{"originalSequence":"RTLR","alternativeSequences":["ERLA"]}},{"type":"Mutagenesis","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Derepression of proV and bgl expression, normal DNA-binding, normal oligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8913298"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["C"]}},{"type":"Mutagenesis","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Derepression of proV and bgl expression, normal DNA-binding, normal oligomerization. Fragments 1-46 and 1-64 no longer bind Hha.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16650431"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8913298"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["H"]}},{"type":"Mutagenesis","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Abolishes the interaction with Hha.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21600204"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["K"]}},{"type":"Mutagenesis","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Derepression of proV and bgl expression.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8913298"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["C"]}},{"type":"Mutagenesis","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Derepression of proV and bgl expression. 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