ROP_ECOLX
ID ROP_ECOLX Reviewed; 63 AA.
AC P03051;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Regulatory protein rop;
DE AltName: Full=RNA one modulator;
DE Short=ROM;
GN Name=rop;
OS Escherichia coli.
OG Plasmid ColE1, and Plasmid pMB1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=ColE1;
RX PubMed=6183660; DOI=10.1073/pnas.79.20.6313;
RA Cesareni G., Muesing M.A., Polisky B.;
RT "Control of ColE1 DNA replication: the rop gene product negatively affects
RT transcription from the replication primer promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:6313-6317(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=ColE1;
RX PubMed=6304700; DOI=10.1073/pnas.80.11.3232;
RA Som T., Tomizawa J.;
RT "Regulatory regions of ColE1 that are involved in determination of plasmid
RT copy number.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3232-3236(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pMB1;
RX PubMed=383387; DOI=10.1101/sqb.1979.043.01.013;
RA Sutcliffe J.G.;
RT "Complete nucleotide sequence of the Escherichia coli plasmid pBR322.";
RL Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=2223771; DOI=10.1021/bi00484a007;
RA Eberle W., Klaus W., Cesarini G., Sander C., Roesch P.;
RT "Proton nuclear magnetic resonance assignments and secondary structure
RT determination of the ColE1 rop (rom) protein.";
RL Biochemistry 29:7402-7407(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=3681971; DOI=10.1016/0022-2836(87)90039-8;
RA Banner D.W., Kokkinidis M., Tsernoglou D.;
RT "Structure of the ColE1 rop protein at 1.7-A resolution.";
RL J. Mol. Biol. 196:657-675(1987).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS).
RX PubMed=8548455; DOI=10.1038/nsb0196-54;
RA Predki P.F., Agrawal V., Brunger A.T., Regan L.;
RT "Amino-acid substitutions in a surface turn modulate protein stability.";
RL Nat. Struct. Biol. 3:54-58(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS).
RX PubMed=10089502; DOI=10.1107/s0907444998002492;
RA Vlassi M., Dauter Z., Wilson K.S., Kokkinidis M.;
RT "Structural parameters for proteins derived from the atomic resolution
RT (1.09-A) structure of a designed variant of the ColE1 ROP protein.";
RL Acta Crystallogr. D 54:1245-1260(1998).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=1841691; DOI=10.1007/bf01874570;
RA Eberle W., Pastore A., Sander C., Rosch P.;
RT "The structure of ColE1 rop in solution.";
RL J. Biomol. NMR 1:71-82(1991).
CC -!- FUNCTION: Regulates plasmid DNA replication by modulating the
CC initiation of transcription of the primer RNA precursor. Processing of
CC the precursor of the primer, RNAII, is inhibited by hydrogen bonding of
CC RNAII to its complementary sequence in RNAI. ROP increases the affinity
CC of RNAI for RNAII and thus decreases the rate of replication initiation
CC events.
CC -!- SUBUNIT: Antiparallel homodimer.
CC -!- INTERACTION:
CC P03051; P03051: rop; NbExp=2; IntAct=EBI-15786748, EBI-15786748;
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DR EMBL; J01749; AAB59736.1; -; Genomic_DNA.
DR EMBL; J01564; AAA87380.1; -; Genomic_DNA.
DR PIR; A03587; RGECRE.
DR RefSeq; NP_040367.1; NC_001371.1.
DR RefSeq; NP_863575.1; NC_005019.1.
DR RefSeq; WP_000165985.1; NZ_WWEL01000035.1.
DR RefSeq; YP_006940171.1; NC_018997.1.
DR RefSeq; YP_006953570.1; NC_019076.1.
DR RefSeq; YP_007316613.1; NC_019982.1.
DR RefSeq; YP_009071085.1; NC_025178.1.
DR RefSeq; YP_794132.1; NC_008488.1.
DR PDB; 1B6Q; X-ray; 1.80 A; A=1-63.
DR PDB; 1F4M; X-ray; 2.25 A; A/B/C/D/E/F=1-63.
DR PDB; 1F4N; X-ray; 1.90 A; A/B=1-63.
DR PDB; 1GMG; X-ray; 1.90 A; A/B=1-63.
DR PDB; 1GTO; X-ray; 1.82 A; A/B/C=2-62.
DR PDB; 1NKD; X-ray; 1.09 A; A=1-63.
DR PDB; 1QX8; X-ray; 2.02 A; A/B=1-63.
DR PDB; 1ROP; X-ray; 1.70 A; A=1-63.
DR PDB; 1RPO; X-ray; 1.40 A; A=1-63.
DR PDB; 1RPR; NMR; -; A/B=1-63.
DR PDB; 1YO7; X-ray; 2.80 A; A/B=1-63.
DR PDB; 2GHY; X-ray; 2.50 A; A/B=1-63.
DR PDB; 2IJH; X-ray; 1.80 A; A/B/C=1-63.
DR PDB; 2IJI; X-ray; 2.30 A; A=1-63.
DR PDB; 2IJJ; X-ray; 1.90 A; A/B/C=1-63.
DR PDB; 2IJK; X-ray; 1.55 A; A/B=1-63.
DR PDB; 3K79; X-ray; 1.96 A; A=2-63.
DR PDB; 4DO2; X-ray; 1.40 A; A/B=1-63.
DR PDB; 7KAE; X-ray; 1.60 A; A/B=2-57.
DR PDBsum; 1B6Q; -.
DR PDBsum; 1F4M; -.
DR PDBsum; 1F4N; -.
DR PDBsum; 1GMG; -.
DR PDBsum; 1GTO; -.
DR PDBsum; 1NKD; -.
DR PDBsum; 1QX8; -.
DR PDBsum; 1ROP; -.
DR PDBsum; 1RPO; -.
DR PDBsum; 1RPR; -.
DR PDBsum; 1YO7; -.
DR PDBsum; 2GHY; -.
DR PDBsum; 2IJH; -.
DR PDBsum; 2IJI; -.
DR PDBsum; 2IJJ; -.
DR PDBsum; 2IJK; -.
DR PDBsum; 3K79; -.
DR PDBsum; 4DO2; -.
DR PDBsum; 7KAE; -.
DR AlphaFoldDB; P03051; -.
DR BMRB; P03051; -.
DR SMR; P03051; -.
DR DIP; DIP-48900N; -.
DR GeneID; 58316519; -.
DR GeneID; 65400901; -.
DR OMA; CEKLHEQ; -.
DR EvolutionaryTrace; P03051; -.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR InterPro; IPR000769; Regulatory_Rop.
DR InterPro; IPR035962; Rop-like_sf.
DR Pfam; PF01815; Rop; 1.
DR PIRSF; PIRSF003229; Rop_reg; 1.
DR PRINTS; PR00835; ROPREGULATRY.
DR SUPFAM; SSF47380; SSF47380; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Plasmid; Transcription; Transcription regulation.
FT CHAIN 1..63
FT /note="Regulatory protein rop"
FT /id="PRO_0000068439"
FT HELIX 3..28
FT /evidence="ECO:0007829|PDB:1NKD"
FT HELIX 32..56
FT /evidence="ECO:0007829|PDB:1NKD"
SQ SEQUENCE 63 AA; 7228 MW; 0A1986BD29CF6FE4 CRC64;
MTKQEKTALN MARFIRSQTL TLLEKLNELD ADEQADICES LHDHADELYR SCLARFGDDG
ENL
