ID   HNS_SERMA               Reviewed;         135 AA.
AC   P18955;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=DNA-binding protein H-NS;
DE   AltName: Full=Histone-like protein HLP-II;
GN   Name=hns; Synonyms=hnsA;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
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 Hha 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}.
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   PIR; S02775; S02775.
DR   AlphaFoldDB; P18955; -.
DR   SMR; P18955; -.
DR   STRING; 273526.SMDB11_1975; -.
DR   PRIDE; P18955; -.
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..135
FT                   /note="DNA-binding protein H-NS"
FT                   /id="PRO_0000168511"
FT   DNA_BIND        112..117
FT                   /evidence="ECO:0000250|UniProtKB:P0A1S2"
SQ   SEQUENCE   135 AA;  15604 MW;  22992C982417F1BF CRC64;
     MSERLKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEDSQAQAE IEERTRKLQQ
     YREMLIADGI DPNELLQTMA ANKAAGKAKR ARRPAKYQYK DENGELKTWT GQGRTPAVIK
     KAIEEQGKSL DDFLL