SOPB_ECOLI
ID SOPB_ECOLI Reviewed; 323 AA.
AC P62558; P08867;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Protein SopB;
DE AltName: Full=Plasmid partition protein B;
GN Name=sopB; Synonyms=B; OrderedLocusNames=ECOK12F047;
OS Escherichia coli (strain K12).
OG Plasmid F.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3029390; DOI=10.1016/0022-2836(86)90459-6;
RA Mori H., Kondo A., Ohshima A., Ogura T., Hiraga S.;
RT "Structure and function of the F plasmid genes essential for
RT partitioning.";
RL J. Mol. Biol. 192:1-15(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Eichenlaub R.;
RT "F plasmid DNA complete mini-F region (F coordinates 40.301F to 49.869F).";
RL Submitted (AUG-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / CR63;
RA Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
RT "Complete nucleotide sequence of the F plasmid: its implications for
RT organization and diversification of plasmid genomes.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Control of plasmid partitioning; required to recognize the
CC cis-acting. Binds specifically with the DNA segment containing the sopC
CC region. SopB is trans-acting.
CC -!- MISCELLANEOUS: Overproduction of SopB protein causes IncG
CC incompatibility.
CC -!- SIMILARITY: Belongs to the ParB family. {ECO:0000305}.
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DR EMBL; X04619; CAA28296.1; -; Genomic_DNA.
DR EMBL; M12987; AAA24903.1; -; Genomic_DNA.
DR EMBL; AP001918; BAA97917.1; -; Genomic_DNA.
DR PIR; T00244; T00244.
DR RefSeq; NP_061426.1; NC_002483.1.
DR RefSeq; WP_000817031.1; NZ_SSUW01000063.1.
DR RefSeq; YP_001294715.1; NC_009602.1.
DR PDB; 3KZ5; X-ray; 1.58 A; A/B/E=276-323.
DR PDB; 3MKW; X-ray; 2.99 A; B/P=155-272.
DR PDB; 3MKY; X-ray; 2.86 A; B/P=155-323.
DR PDB; 3MKZ; X-ray; 2.98 A; A/B/N/U=155-272.
DR PDBsum; 3KZ5; -.
DR PDBsum; 3MKW; -.
DR PDBsum; 3MKY; -.
DR PDBsum; 3MKZ; -.
DR AlphaFoldDB; P62558; -.
DR SMR; P62558; -.
DR PRIDE; P62558; -.
DR EvolutionaryTrace; P62558; -.
DR PRO; PR:P62558; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR DisProt; DP02863; -.
DR InterPro; IPR004437; ParB/RepB/Spo0J.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR InterPro; IPR040873; SoPB_HTH.
DR Pfam; PF02195; ParBc; 1.
DR Pfam; PF18090; SoPB_HTH; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 1.
DR TIGRFAMs; TIGR00180; parB_part; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Plasmid; Plasmid partition.
FT CHAIN 1..323
FT /note="Protein SopB"
FT /id="PRO_0000068408"
FT DNA_BIND 180..199
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:3MKY"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:3MKY"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:3MKY"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:3MKY"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:3MKY"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3MKY"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3MKY"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:3MKY"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3MKY"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:3MKY"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:3MKY"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3MKY"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3KZ5"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:3KZ5"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:3KZ5"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:3KZ5"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:3KZ5"
SQ SEQUENCE 323 AA; 35372 MW; 3CC19C873CED3C1C CRC64;
MKRAPVIPKH TLNTQPVEDT SLSTPAAPMV DSLIARVGVM ARGNAITLPV CGRDVKFTLE
VLRGDSVEKT SRVWSGNERD QELLTEDALD DLIPSFLLTG QQTPAFGRRV SGVIEIADGS
RRRKAAALTE SDYRVLVGEL DDEQMAALSR LGNDYRPTSA YERGQRYASR LQNEFAGNIS
ALADAENISR KIITRCINTA KLPKSVVALF SHPGELSARS GDALQKAFTD KEELLKQQAS
NLHEQKKAGV IFEAEEVITL LTSVLKTSSA SRTSLSSRHQ FAPGATVLYK GDKMVLNLDR
SRVPTECIEK IEAILKELEK PAP