ID   HNS_SALT1               Reviewed;         137 AA.
AC   A0A0F6B244;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=DNA-binding protein H-NS;
GN   Name=hns; OrderedLocusNames=STM14_2116;
OS   Salmonella typhimurium (strain 14028s / SGSC 2262).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=588858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=19897643; DOI=10.1128/jb.01233-09;
RA   Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT   "Short-term signatures of evolutionary change in the Salmonella enterica
RT   serovar typhimurium 14028 genome.";
RL   J. Bacteriol. 192:560-567(2010).
RN   [2]
RP   FUNCTION IN SILENCING AT-RICH DNA, REGULON, AND DISRUPTION PHENOTYPE.
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=16763111; DOI=10.1126/science.1128794;
RA   Navarre W.W., Porwollik S., Wang Y., McClelland M., Rosen H., Libby S.J.,
RA   Fang F.C.;
RT   "Selective silencing of foreign DNA with low GC content by the H-NS protein
RT   in Salmonella.";
RL   Science 313:236-238(2006).
CC   -!- FUNCTION: A DNA-binding protein implicated in transcriptional
CC       repression and chromosome organization and compaction. Binds AT-rich
CC       DNA, repressing its transcription; about 754/4438 tested genes (15%)
CC       bind to H-NS, 70% of these are AT-rich and correspond to horizontally
CC       transferred geness (HTG), thus playing a central role in silencing
CC       foreign genes (PubMed:16763111). This offers the selective advantage of
CC       silencing foreign DNA (PubMed:16763111). Binds nucleation sites in AT-
CC       rich DNA and bridges them, forming higher-order nucleoprotein complexes
CC       and condensing the chromosome (By similarity). A subset of genes are
CC       repressed by H-NS in association with Hha and/or YdgT (By similarity).
CC       {ECO:0000250|UniProtKB:P0ACF8, ECO:0000269|PubMed:16763111}.
CC   -!- SUBUNIT: Homodimer that oligomerizes on DNA into higher-order complexes
CC       that form bridges between disparate regions of DNA compacting it.
CC       Interacts with Hha, YdgT and StpA. {ECO:0000250|UniProtKB:P0ACF8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC       {ECO:0000250|UniProtKB:P0ACF8}.
CC   -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted unless additional
CC       mutations in rpoS and/or phoP are present; hns-rpoS or hns-phoP mutants
CC       grow slowly while triple mutants grow like wild-type. In a double hns-
CC       rpoS mutant 178 genes are down-regulated while 409/4529 were up-
CC       regulated compared to wild-type. {ECO:0000269|PubMed:16763111}.
CC   -!- SIMILARITY: Belongs to the histone-like protein H-NS family.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001363; ACY88582.1; -; Genomic_DNA.
DR   RefSeq; WP_001287383.1; NZ_CP043402.1.
DR   AlphaFoldDB; A0A0F6B244; -.
DR   SMR; A0A0F6B244; -.
DR   EnsemblBacteria; ACY88582; ACY88582; STM14_2116.
DR   GeneID; 66756227; -.
DR   KEGG; seo:STM14_2116; -.
DR   PATRIC; fig|588858.6.peg.1994; -.
DR   HOGENOM; CLU_117503_0_0_6; -.
DR   OMA; NGVEKTW; -.
DR   BioCyc; SENT588858:STM14_RS09650-MON; -.
DR   Proteomes; UP000002695; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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   Coiled coil; Cytoplasm; DNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..137
FT                   /note="DNA-binding protein H-NS"
FT                   /id="PRO_0000436893"
FT   DNA_BIND        112..117
FT                   /evidence="ECO:0000250|UniProtKB:P0A1S2"
FT   COILED          13..65
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   137 AA;  15543 MW;  A9620E5CC7DD3EB1 CRC64;
     MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE VEERTRKLQQ
     YREMLIADGI DPNELLNSMA AAKSGTKAKR AARPAKYSYV DENGETKTWT GQGRTPAVIK
     KAMEEQGKQL EDFLIKE