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Protein

Regulatory protein rop

Gene

rop

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events.

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein rop
Alternative name(s):
RNA one modulator
Short name:
ROM
Gene namesi
Name:rop
Encoded oniPlasmid ColE12 Publications
Plasmid pMB11 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6363Regulatory protein ropPRO_0000068439Add
BLAST

Interactioni

Subunit structurei

Antiparallel homodimer.

Protein-protein interaction databases

DIPiDIP-48900N.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2826Combined sources
Helixi32 – 5625Combined sources
Helixi58 – 636Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B6QX-ray1.80A1-63[»]
1F4MX-ray2.25A/B/C/D/E/F1-63[»]
1F4NX-ray1.90A/B1-63[»]
1GMGX-ray1.90A/B1-63[»]
1GTOX-ray1.82A/B/C2-62[»]
1NKDX-ray1.09A1-63[»]
1QX8X-ray2.02A/B1-63[»]
1ROPX-ray1.70A1-63[»]
1RPOX-ray1.40A1-63[»]
1RPRNMR-A/B1-63[»]
1YO7X-ray2.80A/B1-63[»]
2GHYX-ray2.50A/B1-63[»]
2IJHX-ray1.80A/B/C1-63[»]
2IJIX-ray2.30A1-63[»]
2IJJX-ray1.90A/B/C1-63[»]
2IJKX-ray1.55A/B1-63[»]
3K79X-ray1.96A2-63[»]
4DO2X-ray1.40A/B1-63[»]
ProteinModelPortaliP03051.
SMRiP03051. Positions 1-63.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03051.

Family & Domainsi

Family and domain databases

InterProiIPR000769. Regulatory_Rop.
[Graphical view]
PfamiPF01815. Rop. 1 hit.
[Graphical view]
PIRSFiPIRSF003229. Rop_reg. 1 hit.
PRINTSiPR00835. ROPREGULATRY.
ProDomiPD012167. Rop_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47380. SSF47380. 1 hit.

Sequencei

Sequence statusi: Complete.

P03051-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKQEKTALN MARFIRSQTL TLLEKLNELD ADEQADICES LHDHADELYR
60
SCLARFGDDG ENL
Length:63
Mass (Da):7,228
Last modified:July 21, 1986 - v1
Checksum:i0A1986BD29CF6FE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01749 Genomic DNA. Translation: AAB59736.1.
J01564 Genomic DNA. Translation: AAA87380.1.
PIRiA03587. RGECRE.
RefSeqiNP_040367.1. NC_001371.1.
NP_863575.1. NC_005019.1.
YP_006940171.1. NC_018997.1.
YP_006953570.1. NC_019076.1.
YP_007316613.1. NC_019982.1.
YP_009071085.1. NC_025178.1.
YP_794132.1. NC_008488.1.

Genome annotation databases

GeneIDi13877151.
13906508.
14401266.
1446623.
20493156.
2693963.
4397513.
KEGGipg:13877151.
pg:13906508.
pg:14401266.
pg:1446623.
pg:20493156.
pg:2693963.
pg:4397513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01749 Genomic DNA. Translation: AAB59736.1.
J01564 Genomic DNA. Translation: AAA87380.1.
PIRiA03587. RGECRE.
RefSeqiNP_040367.1. NC_001371.1.
NP_863575.1. NC_005019.1.
YP_006940171.1. NC_018997.1.
YP_006953570.1. NC_019076.1.
YP_007316613.1. NC_019982.1.
YP_009071085.1. NC_025178.1.
YP_794132.1. NC_008488.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B6QX-ray1.80A1-63[»]
1F4MX-ray2.25A/B/C/D/E/F1-63[»]
1F4NX-ray1.90A/B1-63[»]
1GMGX-ray1.90A/B1-63[»]
1GTOX-ray1.82A/B/C2-62[»]
1NKDX-ray1.09A1-63[»]
1QX8X-ray2.02A/B1-63[»]
1ROPX-ray1.70A1-63[»]
1RPOX-ray1.40A1-63[»]
1RPRNMR-A/B1-63[»]
1YO7X-ray2.80A/B1-63[»]
2GHYX-ray2.50A/B1-63[»]
2IJHX-ray1.80A/B/C1-63[»]
2IJIX-ray2.30A1-63[»]
2IJJX-ray1.90A/B/C1-63[»]
2IJKX-ray1.55A/B1-63[»]
3K79X-ray1.96A2-63[»]
4DO2X-ray1.40A/B1-63[»]
ProteinModelPortaliP03051.
SMRiP03051. Positions 1-63.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48900N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi13877151.
13906508.
14401266.
1446623.
20493156.
2693963.
4397513.
KEGGipg:13877151.
pg:13906508.
pg:14401266.
pg:1446623.
pg:20493156.
pg:2693963.
pg:4397513.

Miscellaneous databases

EvolutionaryTraceiP03051.

Family and domain databases

InterProiIPR000769. Regulatory_Rop.
[Graphical view]
PfamiPF01815. Rop. 1 hit.
[Graphical view]
PIRSFiPIRSF003229. Rop_reg. 1 hit.
PRINTSiPR00835. ROPREGULATRY.
ProDomiPD012167. Rop_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47380. SSF47380. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Control of ColE1 DNA replication: the rop gene product negatively affects transcription from the replication primer promoter."
    Cesareni G., Muesing M.A., Polisky B.
    Proc. Natl. Acad. Sci. U.S.A. 79:6313-6317(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Plasmid: ColE1
  2. "Regulatory regions of ColE1 that are involved in determination of plasmid copy number."
    Som T., Tomizawa J.
    Proc. Natl. Acad. Sci. U.S.A. 80:3232-3236(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Plasmid: ColE1
  3. "Complete nucleotide sequence of the Escherichia coli plasmid pBR322."
    Sutcliffe J.G.
    Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Plasmid: pMB1
  4. "Proton nuclear magnetic resonance assignments and secondary structure determination of the ColE1 rop (rom) protein."
    Eberle W., Klaus W., Cesarini G., Sander C., Roesch P.
    Biochemistry 29:7402-7407(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  5. "Structure of the ColE1 rop protein at 1.7-A resolution."
    Banner D.W., Kokkinidis M., Tsernoglou D.
    J. Mol. Biol. 196:657-675(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  6. "Amino-acid substitutions in a surface turn modulate protein stability."
    Predki P.F., Agrawal V., Brunger A.T., Regan L.
    Nat. Struct. Biol. 3:54-58(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS).
  7. "Structural parameters for proteins derived from the atomic resolution (1.09-A) structure of a designed variant of the ColE1 ROP protein."
    Vlassi M., Dauter Z., Wilson K.S., Kokkinidis M.
    Acta Crystallogr. D 54:1245-1260(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS).
  8. Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiROP_ECOLX
AccessioniPrimary (citable) accession number: P03051
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 1, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.