ID   HNS_YEREN               Reviewed;         136 AA.
AC   P0DOA5;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=DNA-binding protein H-NS;
GN   Name=hns {ECO:0000303|PubMed:11790731};
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-27, FUNCTION, AND
RP   INTERACTION WITH YMOA.
RC   STRAIN=DSM 9499 / NCTC 11174 / Y754;
RX   PubMed=11790731; DOI=10.1128/jb.184.3.629-635.2002;
RA   Nieto J.M., Madrid C., Miquelay E., Parra J.L., Rodriguez S., Juarez A.;
RT   "Evidence for direct protein-protein interaction between members of the
RT   enterobacterial Hha/YmoA and H-NS families of proteins.";
RL   J. Bacteriol. 184:629-635(2002).
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 YmoA (By similarity). Complements a number of hns
CC       deficiencies in E.coli; represses the bgl operon, represses hemolysin
CC       expression (PubMed:11790731). {ECO:0000250|UniProtKB:P0ACF8,
CC       ECO:0000269|PubMed:11790731}.
CC   -!- SUBUNIT: Interacts with YmoA in the absence of DNA (PubMed:11790731).
CC       Homodimer that oligomerizes on DNA into higher-order complexes that
CC       form bridges between disparate regions of DNA compacting it. Interacts
CC       with YmoA. {ECO:0000250|UniProtKB:P0ACF8, ECO:0000269|PubMed:11790731}.
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   EMBL; AJ302081; CAC24849.1; -; Genomic_DNA.
DR   RefSeq; WP_005169306.1; NZ_UHIX01000001.1.
DR   AlphaFoldDB; P0DOA5; -.
DR   SMR; P0DOA5; -.
DR   STRING; 1443113.LC20_02539; -.
DR   GeneID; 67418433; -.
DR   eggNOG; COG2916; Bacteria.
DR   OMA; NGVEKTW; -.
DR   OrthoDB; 1911889at2; -.
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; Direct protein sequencing; DNA-binding; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..136
FT                   /note="DNA-binding protein H-NS"
FT                   /id="PRO_0000436896"
FT   DNA_BIND        113..118
FT                   /evidence="ECO:0000250|UniProtKB:P0A1S2"
FT   COILED          13..67
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   136 AA;  15509 MW;  414D35EBE8971C0E CRC64;
     MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEDSQAQAE IEERTRKLQQ
     YREMLIADGI DPNELLNAMA VTKAAATKSK RAARPAKYKY IDENGETKTW TGQGRTPAVI
     KKAIEEQGKS LDDFLL