STPA_SALTY
ID STPA_SALTY Reviewed; 133 AA.
AC P0A1S4; O33800;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DNA-binding protein StpA;
DE AltName: Full=H-NS homolog StpA;
GN Name=stpA; OrderedLocusNames=STM2799;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Sonnenfield J.M., Raupach B., Falkow S., Higgins C.F., Hinton J.C.D.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: A DNA-binding protein that acts in a fashion similar to H-NS,
CC repressing gene transcription. A subset of H-NS/StpA-regulated genes
CC require auxillary proteins for repression; these auxillary proteins
CC (Hha and other similar proteins) may also modulate oligomerization of
CC the H-NS/StpA complex (By similarity). {ECO:0000250|UniProtKB:P0ACG1}.
CC -!- SUBUNIT: Forms homodimers, can interact with H-NS.
CC {ECO:0000250|UniProtKB:P0ACG1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000250|UniProtKB:P0ACG1}.
CC -!- SIMILARITY: Belongs to the histone-like protein H-NS family.
CC {ECO:0000305}.
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DR EMBL; AF009363; AAB63588.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21684.1; -; Genomic_DNA.
DR RefSeq; NP_461725.1; NC_003197.2.
DR RefSeq; WP_001051100.1; NC_003197.2.
DR AlphaFoldDB; P0A1S4; -.
DR SMR; P0A1S4; -.
DR STRING; 99287.STM2799; -.
DR PaxDb; P0A1S4; -.
DR EnsemblBacteria; AAL21684; AAL21684; STM2799.
DR GeneID; 1254322; -.
DR KEGG; stm:STM2799; -.
DR PATRIC; fig|99287.12.peg.2955; -.
DR HOGENOM; CLU_117503_0_0_6; -.
DR OMA; NTWLELM; -.
DR PhylomeDB; P0A1S4; -.
DR BioCyc; SENT99287:STM2799-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0003681; F:bent DNA binding; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IBA:GO_Central.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..133
FT /note="DNA-binding protein StpA"
FT /id="PRO_0000168516"
FT DNA_BIND 111..116
FT /evidence="ECO:0000250|UniProtKB:P0A1S2"
FT REGION 81..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 133 AA; 15488 MW; 86861AA6ED6E1AFB CRC64;
MNLMLQNLNN IRTLRAMARE FSIDVLEEML EKFRVVTKER REEEELQQRQ LAEKQEKINA
FLELMKADGI NPEELFAMDS AMPRSAKKRQ PRPAKYRFTD FNGEEKTWTG QGRTPKPIAQ
ALAAGKSLDD FLI