BV3F_BURVG
ID BV3F_BURVG Reviewed; 112 AA.
AC A4JS72;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=DNA-binding protein Bv3F {ECO:0000303|PubMed:21673140};
GN OrderedLocusNames=Bcep1808_6219, Bcep1808_7148;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OG Plasmid pBVIE02.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486; PLASMID=pBVIE02;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of plasmid pBVIE02 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE BY NMR OF 71-112, FUNCTION, AND MUTAGENESIS OF 89-ARG--ARG-91.
RX PubMed=21673140; DOI=10.1073/pnas.1102544108;
RA Gordon B.R., Li Y., Cote A., Weirauch M.T., Ding P., Hughes T.R.,
RA Navarre W.W., Xia B., Liu J.;
RT "Structural basis for recognition of AT-rich DNA by unrelated xenogeneic
RT silencing proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10690-10695(2011).
CC -!- FUNCTION: A DNA-binding protein implicated in transcriptional
CC repression and chromosome organization and compaction. Binds in the
CC minor groove of AT-rich DNA (PubMed:21673140). Binds nucleation sites
CC in AT-rich DNA and bridges them, forming higher-order nucleoprotein
CC complexes and condensing the chromosome. As many horizontally
CC transferred genes are AT-rich, it plays a central role in silencing
CC foreign genes (By similarity). {ECO:0000250|UniProtKB:P0ACF8,
CC ECO:0000269|PubMed:21673140}.
CC -!- SUBUNIT: Homodimer that oligomerizes on DNA into higher-order complexes
CC that form bridges between disparate regions of DNA compacting it (By
CC similarity). {ECO:0000250|UniProtKB:P0ACF8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000250|UniProtKB:P0ACF8}.
CC -!- MISCELLANEOUS: Encoded on chromosome 3 and plasmid pBVIE02.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone-like protein H-NS family.
CC {ECO:0000305}.
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DR EMBL; CP000616; ABO59125.1; -; Genomic_DNA.
DR EMBL; CP000618; ABO60030.1; -; Genomic_DNA.
DR PDB; 2L92; NMR; -; A=71-112.
DR PDBsum; 2L92; -.
DR AlphaFoldDB; A4JS72; -.
DR SMR; A4JS72; -.
DR STRING; 269482.Bcep1808_6219; -.
DR EnsemblBacteria; ABO59125; ABO59125; Bcep1808_6219.
DR EnsemblBacteria; ABO60030; ABO60030; Bcep1808_7148.
DR KEGG; bvi:Bcep1808_6219; -.
DR KEGG; bvi:Bcep1808_7148; -.
DR eggNOG; COG2916; Bacteria.
DR HOGENOM; CLU_117503_5_1_4; -.
DR OMA; GRENMDP; -.
DR Proteomes; UP000002287; Chromosome 3.
DR Proteomes; UP000002287; Plasmid pBVIE02.
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:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR027444; H-NS_C_dom.
DR InterPro; IPR001801; Histone_HNS.
DR Pfam; PF00816; Histone_HNS; 1.
DR SMART; SM00528; HNS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Plasmid; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..112
FT /note="DNA-binding protein Bv3F"
FT /id="PRO_0000436897"
FT DNA_BIND 89..95
FT /evidence="ECO:0000269|PubMed:21673140"
FT DNA_BIND 89..94
FT /evidence="ECO:0000250|UniProtKB:P0A1S2"
FT REGION 65..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 89..91
FT /note="RGR->AGA: Loss of DNA-binding, in fragment 71-112."
FT /evidence="ECO:0000269|PubMed:21673140"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2L92"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2L92"
SQ SEQUENCE 112 AA; 12513 MW; CCAA9BAF346541F0 CRC64;
MPVQGRENMD PKSPGYLALI AQRESLDAQI IAARKAEREV AIGQIKALMK EFDLSVLDLQ
ERVQKRNSKR MSTVPKYRDP ATGKTWSGRG RQPAWLGNDP AAFLIQPDLP AI
