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P03051 (ROP_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulatory protein rop
Alternative name(s):
RNA one modulator
Short name=ROM
Gene names
Name:rop
Encoded onPlasmid ColE1 Ref.1 Ref.2
Plasmid pMB1 Ref.3
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length63 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Antiparallel homodimer.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6363Regulatory protein rop
PRO_0000068439

Secondary structure

...... 63
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03051 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0A1986BD29CF6FE4

FASTA637,228
        10         20         30         40         50         60 
MTKQEKTALN MARFIRSQTL TLLEKLNELD ADEQADICES LHDHADELYR SCLARFGDDG 


ENL 

« Hide

References

[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(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete nucleotide sequence of the Escherichia coli plasmid pBR322."
Sutcliffe J.G.
Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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(1990) [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(1987) [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(1996) [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(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS).
[8]"The structure of ColE1 rop in solution."
Eberle W., Pastore A., Sander C., Rosch P.
J. Biomol. NMR 1:71-82(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01749 Genomic DNA. Translation: AAB59736.1.
J01564 Genomic DNA. Translation: AAA87380.1.
PIRRGECRE. A03587.
RefSeqNP_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_794132.1. NC_008488.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP03051.
SMRP03051. Positions 1-63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48900N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13877151.
13906508.
14401266.
1446623.
2693963.
4397513.

Family and domain databases

InterProIPR000769. Regulatory_Rop.
[Graphical view]
PfamPF01815. Rop. 1 hit.
[Graphical view]
PIRSFPIRSF003229. Rop_reg. 1 hit.
PRINTSPR00835. ROPREGULATRY.
ProDomPD012167. Rop_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47380. SSF47380. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP03051.

Entry information

Entry nameROP_ECOLX
AccessionPrimary (citable) accession number: P03051
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references