HNS_ECOL6
ID HNS_ECOL6 Reviewed; 137 AA.
AC P0ACF9; P08936;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DNA-binding protein H-NS;
DE AltName: Full=Histone-like protein HLP-II;
DE AltName: Full=Protein B1;
DE AltName: Full=Protein H1;
GN Name=hns; OrderedLocusNames=c1701;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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 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, Cnu and StpA. {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 EMBL; AE014075; AAN80168.1; -; Genomic_DNA.
DR RefSeq; WP_001287378.1; NC_004431.1.
DR AlphaFoldDB; P0ACF9; -.
DR BMRB; P0ACF9; -.
DR SMR; P0ACF9; -.
DR STRING; 199310.c1701; -.
DR EnsemblBacteria; AAN80168; AAN80168; c1701.
DR GeneID; 66674941; -.
DR KEGG; ecc:c1701; -.
DR eggNOG; COG2916; Bacteria.
DR HOGENOM; CLU_117503_0_0_6; -.
DR OMA; NGVEKTW; -.
DR BioCyc; ECOL199310:C1701-MON; -.
DR Proteomes; UP000001410; 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 3: Inferred from homology;
KW Cytoplasm; DNA-binding; Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..137
FT /note="DNA-binding protein H-NS"
FT /id="PRO_0000168505"
FT DNA_BIND 112..117
FT /evidence="ECO:0000250|UniProtKB:P0A1S2"
FT SITE 12
FT /note="Interacts with Hha"
FT /evidence="ECO:0000250"
SQ SEQUENCE 137 AA; 15540 MW; E628184AC7C86F49 CRC64;
MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE VEERTRKLQQ
YREMLIADGI DPNELLNSLA AVKSGTKAKR AQRPAKYSYV DENGETKTWT GQGRTPAVIK
KAMDEQGKSL DDFLIKQ
