HNS_SALTY
ID HNS_SALTY Reviewed; 137 AA.
AC P0A1S2; P17428;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=DNA-binding protein H-NS {ECO:0000303|PubMed:2171779};
DE AltName: Full=Histone-like protein HLP-II;
DE AltName: Full=Protein B1;
DE AltName: Full=Protein H1 {ECO:0000303|PubMed:2171779};
GN Name=hns; Synonyms=hnsA, osmZ {ECO:0000303|PubMed:2171779};
GN OrderedLocusNames=STM1751;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2113274; DOI=10.1093/nar/18.11.3397;
RA Marsh M., Hillyard D.R.;
RT "Nucleotide sequence of hns encoding the DNA-binding protein H-NS of
RT Salmonella typhimurium.";
RL Nucleic Acids Res. 18:3397-3397(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2171779; DOI=10.1016/0092-8674(90)90458-q;
RA Hulton C.S.J., Seirafi A., Hinton J.C.D., Sidebotham J.M., Waddell L.,
RA Pavitt G.D., Owen-Hughes T., Spassky A., Buc H., Higgins C.F.;
RT "Histone-like protein H1 (H-NS), DNA supercoiling, and gene expression in
RT bacteria.";
RL Cell 63:631-642(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=1423593; DOI=10.1016/0092-8674(92)90354-f;
RA Owen-Hughes T.A., Pavitt G.D., Santos D.S., Sidebotham J.M., Hulton C.S.,
RA Hinton J.C., Higgins C.F.;
RT "The chromatin-associated protein H-NS interacts with curved DNA to
RT influence DNA topology and gene expression.";
RL Cell 71:255-265(1992).
RN [5]
RP FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS OF CYS-21, COILED COIL, AND
RP DNA-BINDING.
RX PubMed=10844682; DOI=10.1046/j.1365-2958.2000.01917.x;
RA Smyth C.P., Lundbaeck T., Renzoni D., Siligardi G., Beavil R., Layton M.,
RA Sidebotham J.M., Hinton J.C., Driscoll P.C., Higgins C.F., Ladbury J.E.;
RT "Oligomerization of the chromatin-structuring protein H-NS.";
RL Mol. Microbiol. 36:962-972(2000).
RN [6]
RP FUNCTION IN SILENCING FOREIGN AT-RICH DNA, REGULON, DISRUPTION PHENOTYPE,
RP AND DNA-BINDING.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=16933988; DOI=10.1371/journal.ppat.0020081;
RA Lucchini S., Rowley G., Goldberg M.D., Hurd D., Harrison M., Hinton J.C.;
RT "H-NS mediates the silencing of laterally acquired genes in bacteria.";
RL PLoS Pathog. 2:E81-E81(2006).
RN [7]
RP STRUCTURE BY NMR OF 1-64, DOMAIN, AND COILED COIL.
RX PubMed=11237622; DOI=10.1006/jmbi.2001.4471;
RA Renzoni D., Esposito D., Pfuhl M., Hinton J.C., Higgins C.F.,
RA Driscoll P.C., Ladbury J.E.;
RT "Structural characterization of the N-terminal oligomerization domain of
RT the bacterial chromatin-structuring protein, H-NS.";
RL J. Mol. Biol. 306:1127-1137(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 1-83, POSSIBLE MODE OF DNA
RP PACKING, AND SUBUNIT.
RX PubMed=20798056; DOI=10.1073/pnas.1006966107;
RA Arold S.T., Leonard P.G., Parkinson G.N., Ladbury J.E.;
RT "H-NS forms a superhelical protein scaffold for DNA condensation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15728-15732(2010).
RN [9]
RP STRUCTURE BY NMR OF 91-137, FUNCTION, DNA-BINDING, AND MUTAGENESIS OF
RP GLU-102; 112-GLN--ARG-114; GLN-112 AND ARG-114.
RX PubMed=21673140; DOI=10.1073/pnas.1102544108;
RA Gordon B.R., Li Y., Cote A., Weirauch M.T., Ding P., Hughes T.R.,
RA Navarre W.W., Xia B., Liu J.;
RT "Structural basis for recognition of AT-rich DNA by unrelated xenogeneic
RT silencing proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10690-10695(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 3-46 IN COMPLEX WITH HHA,
RP SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, DNA-BINDING, AND MUTAGENESIS OF
RP ILE-11 AND ARG-12.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=23515315; DOI=10.1074/jbc.m113.455378;
RA Ali S.S., Whitney J.C., Stevenson J., Robinson H., Howell P.L.,
RA Navarre W.W.;
RT "Structural insights into the regulation of foreign genes in Salmonella by
RT the Hha/H-NS complex.";
RL J. Biol. Chem. 288:13356-13369(2013).
RN [11]
RP REVIEW.
RX PubMed=25638302; DOI=10.1016/j.mib.2015.01.009;
RA Landick R., Wade J.T., Grainger D.C.;
RT "H-NS and RNA polymerase: a love-hate relationship?";
RL Curr. Opin. Microbiol. 24:53-59(2015).
CC -!- FUNCTION: Binds tightly to dsDNA (PubMed:10844682). Acts as a global
CC transcriptional regulator through its ability to bind to AT-rich DNA
CC sequences (PubMed:1423593, PubMed:16933988, PubMed:21673140). Binds in
CC the minor groove of AT-rich DNA (PubMed:21673140). Was found to bind
CC 746 genes, about half of which show no change in expression in
CC disruption experiments suggesting these sites are important for
CC nucleoid structure (PubMed:16933988). On a global level genes bound by
CC H-NS are expressed at a lower than average level; H-NS is excluded from
CC binding to highly transcribed genes and does not co-localize with RNA
CC polymerase in DNA-binding studies during exponential growth in rich
CC medium (PubMed:16933988). The best correlation for H-NS binding is AT-
CC content rather than predicted DNA curvature (PubMed:16933988). Has a
CC strong preference for DNA that has been recently acquired by horizontal
CC gene transfer, binding strongly to Salmonella pathogenicity islands 1
CC and 2 (SPI1 and SPI2); this offers the selective advantage of silencing
CC foreign DNA while keeping it in the genome in case of need
CC (PubMed:16933988). DNA-binding influences plasmid DNA topology
CC (PubMed:1423593). For the proU locus (the proV-proW-proX operon)
CC inhibits transcription at low osmolarity by binding to AT-rich, curved,
CC DNA downstream of the transcription start site of proV; repression is
CC greater when more than 1 curved DNA sequence is present
CC (PubMed:1423593). It plays a role in the thermal control of pili
CC production (By similarity). It is subject to transcriptional auto-
CC repression (By similarity). It binds preferentially to the upstream
CC region of its own gene recognizing two segments of DNA on both sides of
CC a bend centered around -150 (By similarity).
CC {ECO:0000250|UniProtKB:P0ACF8, ECO:0000269|PubMed:10844682,
CC ECO:0000269|PubMed:1423593, ECO:0000269|PubMed:16933988,
CC ECO:0000269|PubMed:21673140}.
CC -!- SUBUNIT: Forms oligomers of increasing size with increasing protein
CC concentration (PubMed:10844682, PubMed:23515315). The fragment of 1-83
CC probably forms oligomers of 4 dimeric units at 10 degrees Celsius, at
CC 40 degrees Celsius only dimers are formed (PubMed:20798056). Binds Hha
CC and YdgT (also known as cnu); crystal structures suggest each H-NS
CC dimer could bind 2 Hha monomers on opposites sides (PubMed:23515315).
CC Probably also binds StpA (By similarity).
CC {ECO:0000250|UniProtKB:P0ACF8, ECO:0000269|PubMed:10844682,
CC ECO:0000269|PubMed:20798056, ECO:0000269|PubMed:23515315}.
CC -!- INTERACTION:
CC P0A1S2; P0A1S2: hns; NbExp=2; IntAct=EBI-15873459, EBI-15873459;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000250|UniProtKB:P0ACF8}.
CC -!- DOMAIN: Composed of 2 domains (approximately residues 1-64 and 89-136)
CC joined by a flexible linker. The isolated N-terminus (1-64) forms a
CC trimer, probably via coiled-coil interactions (PubMed:10844682,
CC PubMed:11237622). The isolated N-terminus plus linker fragment
CC (residues 1-89) forms homooligomers of increasing size with increasing
CC protein concentration, while the isolated C-terminus fragment is a
CC monomer (PubMed:10844682). A shorter fragment (residues 1-46) interacts
CC with Hha (PubMed:23515315). {ECO:0000269|PubMed:10844682,
CC ECO:0000269|PubMed:11237622, ECO:0000269|PubMed:23515315}.
CC -!- DISRUPTION PHENOTYPE: Loss of osmotic regulation of the proU locus,
CC loss of changes in plasmid linking number (PubMed:1423593). 2X
CC decreased growth rate, which is partially restored by a mutation
CC preventing expression of SPI2, increased expression of about half of
CC the genes to which H-NS binds (PubMed:16933988). Note strain LT2 has
CC point mutation in rpoS which decreases its translation efficiency, in
CC the presence of wild-type rpoS, deletion of hns is lethal
CC (PubMed:16933988). {ECO:0000269|PubMed:1423593,
CC ECO:0000269|PubMed:16933988}.
CC -!- SIMILARITY: Belongs to the histone-like protein H-NS family.
CC {ECO:0000305}.
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DR EMBL; M37891; AAB61148.1; -; Genomic_DNA.
DR EMBL; X14375; CAA32549.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20669.1; -; Genomic_DNA.
DR PIR; S10155; S10155.
DR RefSeq; NP_460710.1; NC_003197.2.
DR RefSeq; WP_001287383.1; NC_003197.2.
DR PDB; 2L93; NMR; -; A=91-137.
DR PDB; 3NR7; X-ray; 3.70 A; A/B=1-83.
DR PDB; 4ICG; X-ray; 2.92 A; A/B=3-46.
DR PDBsum; 2L93; -.
DR PDBsum; 3NR7; -.
DR PDBsum; 4ICG; -.
DR AlphaFoldDB; P0A1S2; -.
DR BMRB; P0A1S2; -.
DR SMR; P0A1S2; -.
DR DIP; DIP-59374N; -.
DR STRING; 99287.STM1751; -.
DR PaxDb; P0A1S2; -.
DR EnsemblBacteria; AAL20669; AAL20669; STM1751.
DR GeneID; 1253270; -.
DR GeneID; 66756227; -.
DR KEGG; stm:STM1751; -.
DR PATRIC; fig|99287.12.peg.1847; -.
DR HOGENOM; CLU_117503_0_0_6; -.
DR OMA; NGVEKTW; -.
DR PhylomeDB; P0A1S2; -.
DR BioCyc; SENT99287:STM1751-MON; -.
DR EvolutionaryTrace; P0A1S2; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0003681; F:bent DNA binding; IDA:UniProtKB.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR Gene3D; 1.10.287.1050; -; 1.
DR Gene3D; 4.10.430.10; -; 1.
DR InterPro; IPR027444; H-NS_C_dom.
DR InterPro; IPR037150; H-NS_C_dom_sf.
DR InterPro; IPR001801; Histone_HNS.
DR InterPro; IPR027454; Histone_HNS_N.
DR Pfam; PF00816; Histone_HNS; 1.
DR PIRSF; PIRSF002096; HnS; 1.
DR SMART; SM00528; HNS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; DNA-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0ACF8"
FT CHAIN 2..137
FT /note="DNA-binding protein H-NS"
FT /id="PRO_0000168510"
FT DNA_BIND 112..117
FT /evidence="ECO:0000269|PubMed:21673140"
FT REGION 2..64
FT /note="Responsible for protein oligomerization"
FT /evidence="ECO:0000269|PubMed:10844682"
FT COILED 22..55
FT /evidence="ECO:0000269|PubMed:11237622,
FT ECO:0000305|PubMed:10844682"
FT SITE 12
FT /note="Interacts with Hha"
FT /evidence="ECO:0000250"
FT MUTAGEN 11
FT /note="I->A: No longer binds Hha or YdgT, slightly altered
FT DNA-binding, wild-type self-association. Derepression of
FT some H-NS-regulated genes, acts similarly to an hha
FT deletion strain."
FT /evidence="ECO:0000269|PubMed:23515315"
FT MUTAGEN 12
FT /note="R->A: No longer binds Hha, still able to bind YdgT."
FT /evidence="ECO:0000269|PubMed:23515315"
FT MUTAGEN 12
FT /note="R->H: No longer binds Hha or YdgT, slightly altered
FT DNA-binding, may self associate into longer than wild-type
FT filaments. Derepression."
FT /evidence="ECO:0000269|PubMed:23515315"
FT MUTAGEN 21
FT /note="C->S: No effect on DNA-binding or physical
FT properties."
FT /evidence="ECO:0000269|PubMed:10844682"
FT MUTAGEN 102
FT /note="E->A: No change in DNA-binding, in fragment 91-137."
FT /evidence="ECO:0000269|PubMed:21673140"
FT MUTAGEN 112..114
FT /note="QGR->AGA: Loss of DNA-binding, in fragment 91-137."
FT /evidence="ECO:0000269|PubMed:21673140"
FT MUTAGEN 112
FT /note="Q->A: Reduced DNA-binding, in fragment 91-137."
FT /evidence="ECO:0000269|PubMed:21673140"
FT MUTAGEN 114
FT /note="R->A: Considerably reduced DNA-binding, in fragment
FT 91-137."
FT /evidence="ECO:0000269|PubMed:21673140"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4ICG"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:4ICG"
FT HELIX 23..43
FT /evidence="ECO:0007829|PDB:4ICG"
FT STRAND 96..109
FT /evidence="ECO:0007829|PDB:2L93"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:2L93"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2L93"
SQ SEQUENCE 137 AA; 15543 MW; A9620E5CC7DD3EB1 CRC64;
MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE VEERTRKLQQ
YREMLIADGI DPNELLNSMA AAKSGTKAKR AARPAKYSYV DENGETKTWT GQGRTPAVIK
KAMEEQGKQL EDFLIKE
