HNSP_SALTI
ID HNSP_SALTI Reviewed; 134 AA.
AC Q9L5H8;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=DNA-binding protein H-NS, plasmid;
DE AltName: Full=Plasmid R27-encoded H-HS {ECO:0000303|PubMed:19521501};
DE Short=H-NS-R27 {ECO:0000303|PubMed:19521501};
GN Name=hns;
OS Salmonella typhi.
OG Plasmid IncHI1 R27.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncHI1 R27;
RX PubMed=10773089; DOI=10.1093/nar/28.10.2177;
RA Sherburne C.K., Lawley T.D., Gilmour M.W., Blattner F.R., Burland V.,
RA Grotbeck E., Rose D.J., Taylor D.E.;
RT "The complete DNA sequence and analysis of R27, a large IncHI plasmid from
RT Salmonella typhi that is temperature sensitive for transfer.";
RL Nucleic Acids Res. 28:2177-2186(2000).
RN [2]
RP FUNCTION, AND DNA-BINDING.
RC PLASMID=IncHI1 R27;
RX PubMed=19521501; DOI=10.1371/journal.pgen.1000513;
RA Banos R.C., Vivero A., Aznar S., Garcia J., Pons M., Madrid C., Juarez A.;
RT "Differential regulation of horizontally acquired and core genome genes by
RT the bacterial modulator H-NS.";
RL PLoS Genet. 5:E1000513-E1000513(2009).
CC -!- FUNCTION: A DNA-binding protein implicated in transcriptional
CC repression and chromosome organization and compaction. Binds DNA,
CC modifying gene expression, especially non-core genes. Does not regulate
CC the same set of genes as its chromosomal counterpart (tested in
CC S.typhimurium strain SL1344 / SV5015, chromosomal H-NS protein is AC
CC A0A0H3NBY9). Thus it has a not-completely overlapping set of gene
CC targets compared to its chromosomal homolog; many of these target genes
CC are either plasmid-encoded or acquired by horizontally transferred
CC genes (HTG). This protein can function in the absence of H-NS-
CC modulating protein Hha (either chromosomal or plasmid-encoded),
CC although many HTG genes are regulated by an H-NS/Hha complex
CC (PubMed:19521501). Binds nucleation sites in AT-rich DNA and bridges
CC them, forming higher-order nucleoprotein complexes and condensing the
CC chromosome (By similarity). A subset of genes are repressed by H-NS in
CC association with Hha and/or Cnu (ydgT) (By similarity).
CC {ECO:0000250|UniProtKB:P0ACF8, ECO:0000269|PubMed:19521501}.
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 -!- MISCELLANEOUS: This protein is encoded on incompatibility group H
CC (IncHI) plasmid R27, a temperature-sensitive conjugative plasmid.
CC {ECO:0000305|PubMed:10773089}.
CC -!- SIMILARITY: Belongs to the histone-like protein H-NS family.
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DR EMBL; AF250878; AAF70002.1; -; Genomic_DNA.
DR RefSeq; NP_058377.1; NC_002305.1.
DR RefSeq; WP_010892345.1; NC_002305.1.
DR AlphaFoldDB; Q9L5H8; -.
DR SMR; Q9L5H8; -.
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; Plasmid; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..134
FT /note="DNA-binding protein H-NS, plasmid"
FT /id="PRO_0000436895"
FT DNA_BIND 112..117
FT /evidence="ECO:0000250|UniProtKB:P0A1S2"
FT REGION 77..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..67
FT /evidence="ECO:0000255"
SQ SEQUENCE 134 AA; 15208 MW; AFFA374805240ECB CRC64;
MSEALKSLNN IRTLRAQGRE LPLEILEELL EKLSVVVEER RQEESSKEAE LKARLEKIES
LRQLMLEDGI DPEELLSSFS AKSGAPKKVR EPRPAKYKYT DVNGETKTWT GQGRTPKALA
EQLEAGKKLD DFLI