ID   HNS_PROVU               Reviewed;         134 AA.
AC   P18818;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=DNA-binding protein H-NS;
DE   AltName: Full=Histone-like protein HLP-II;
GN   Name=hns; Synonyms=hnsA;
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2494066; DOI=10.1016/0014-5793(89)81156-1;
RA   la Teana A., Falconi M., Scarlato V., Lammi M., Pon C.L.;
RT   "Characterization of the structural genes for the DNA-binding protein H-NS
RT   in Enterobacteriaceae.";
RL   FEBS Lett. 244:34-38(1989).
CC   -!- FUNCTION: A DNA-binding protein implicated in transcriptional
CC       repression and chromosome organization and compaction. Binds nucleation
CC       sites in AT-rich DNA and bridges them, forming higher-order
CC       nucleoprotein complexes and condensing the chromosome. As many
CC       horizontally transferred genes are AT-rich, it plays a central role in
CC       silencing foreign genes. A subset of genes are repressed by H-NS in
CC       association with other proteins (By similarity).
CC       {ECO:0000250|UniProtKB:P0ACF8}.
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 YmoA and other similar proteins.
CC       {ECO:0000250|UniProtKB:P0ACF8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC       {ECO:0000250|UniProtKB:P0ACF8}.
CC   -!- SIMILARITY: Belongs to the histone-like protein H-NS family.
CC       {ECO:0000305}.
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DR   PIR; S02776; S02776.
DR   AlphaFoldDB; P18818; -.
DR   SMR; P18818; -.
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   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Repressor; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACF8"
FT   CHAIN           2..134
FT                   /note="DNA-binding protein H-NS"
FT                   /id="PRO_0000168507"
FT   DNA_BIND        111..116
FT                   /evidence="ECO:0000250|UniProtKB:P0A1S2"
SQ   SEQUENCE   134 AA;  15265 MW;  202C49A8A06597B3 CRC64;
     MSESLKILNN IRTLRAQARE TSLETLEEML EKLEVVVNER REEEQAMQAE IEERQQKLQK
     YRELLIADGI DPTDLLEAAG ASKTGRAKRA ARPAKYSYVD DNGETKTWTG QGRTLAVIKR
     AIEEEGKSLE DFLI