HNS_SALPA
ID HNS_SALPA Reviewed; 137 AA.
AC Q5PCT5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 87.
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; Synonyms=hnsA, osmZ; OrderedLocusNames=SPA1127;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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, YdgT 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}.
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 EMBL; CP000026; AAV77088.1; -; Genomic_DNA.
DR RefSeq; WP_001287382.1; NC_006511.1.
DR AlphaFoldDB; Q5PCT5; -.
DR BMRB; Q5PCT5; -.
DR SMR; Q5PCT5; -.
DR PRIDE; Q5PCT5; -.
DR EnsemblBacteria; AAV77088; AAV77088; SPA1127.
DR KEGG; spt:SPA1127; -.
DR HOGENOM; CLU_117503_0_0_6; -.
DR OMA; NGVEKTW; -.
DR Proteomes; UP000008185; 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_0000168508"
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; 15601 MW; A9620D93C7DD3EB1 CRC64;
MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE VEERTRKLQQ
YREMLIADGI DPNELLNSMA AAKSGTKAKR AARPAKYSYV DENGETKTWT GQGRTPAVIK
KAMEEQDKQL EDFLIKE