HNS_SHIFL
ID HNS_SHIFL Reviewed; 137 AA.
AC P09120;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DNA-binding protein H-NS;
DE AltName: Full=Pathogenesis protein KcpA;
GN Name=hns;
GN Synonyms=hnsA, kcpA {ECO:0000303|PubMed:2668687},
GN virR {ECO:0000303|PubMed:1406252}; OrderedLocusNames=SF1237, S1323;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-137, AND FUNCTION.
RC STRAIN=YSH6200 / Serotype 2a;
RX PubMed=2668687; DOI=10.1111/j.1365-2958.1989.tb01809.x;
RA Yamada M., Sasakawa C., Okada N., Makino S., Yoshikawa M.;
RT "Molecular cloning and characterization of chromosomal virulence region
RT kcpA of Shigella flexneri.";
RL Mol. Microbiol. 3:207-213(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=1406252; DOI=10.1111/j.1365-2958.1992.tb01385.x;
RA Hromockyj A.E., Tucker S.C., Maurelli A.T.;
RT "Temperature regulation of Shigella virulence: identification of the
RT repressor gene virR, an analogue of hns, and partial complementation by
RT tyrosyl transfer RNA (tRNA1(Tyr)).";
RL Mol. Microbiol. 6:2113-2124(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- FUNCTION: KcpA is involved in pathogenesis. The protein is required by
CC invading bacteria for spread into adjacent cells (colonic epithelial
CC cells). It is needed to establish kerato-conjunctivitis provocation
CC (KCP) by pathogenic bacteria (PubMed:2668687). It is involved in the
CC thermal control of epithelial cell invasion (PubMed:1406252).
CC {ECO:0000269|PubMed:1406252, ECO:0000269|PubMed:2668687}.
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 -!- INTERACTION:
CC P09120; P09120: hns; NbExp=2; IntAct=EBI-2011657, EBI-2011657;
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; X66848; CAA47322.1; -; Genomic_DNA.
DR EMBL; X13131; CAA31522.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN42850.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16735.1; -; Genomic_DNA.
DR PIR; S24755; S24755.
DR RefSeq; NP_707143.1; NC_004337.2.
DR RefSeq; WP_001287378.1; NZ_WPGW01000029.1.
DR AlphaFoldDB; P09120; -.
DR BMRB; P09120; -.
DR SMR; P09120; -.
DR IntAct; P09120; 2.
DR STRING; 198214.SF1237; -.
DR PRIDE; P09120; -.
DR EnsemblBacteria; AAN42850; AAN42850; SF1237.
DR EnsemblBacteria; AAP16735; AAP16735; S1323.
DR GeneID; 1023363; -.
DR GeneID; 66674941; -.
DR KEGG; sfl:SF1237; -.
DR KEGG; sfx:S1323; -.
DR PATRIC; fig|198214.7.peg.1455; -.
DR HOGENOM; CLU_117503_0_0_6; -.
DR OMA; NGVEKTW; -.
DR OrthoDB; 1911889at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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:0042802; F:identical protein binding; IPI:IntAct.
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 Cytoplasm; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Virulence.
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_0000168512"
FT DNA_BIND 112..117
FT /evidence="ECO:0000250|UniProtKB:P0A1S2"
SQ SEQUENCE 137 AA; 15540 MW; E628184AC7C86F49 CRC64;
MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE VEERTRKLQQ
YREMLIADGI DPNELLNSLA AVKSGTKAKR AQRPAKYSYV DENGETKTWT GQGRTPAVIK
KAMDEQGKSL DDFLIKQ
