P03051 (ROP_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulatory protein rop

Alternative name(s):
RNA one modulator
Short name=ROM

Gene names

Name:

rop

Encoded on

Plasmid ColE1 Ref.1 Ref.2
Plasmid pMB1 Ref.3

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	63 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Keywords
Biological process	Transcription Transcription regulation
Technical term	3D-structure Plasmid
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 63

63

Regulatory protein rop

PRO_0000068439

Secondary structure

1

.

.

.

.

.

63

Helix Strand Turn

Details...

Helix

3 – 28

26

Helix

32 – 56

25

Sequences

	Sequence		Length	Mass (Da)
	P03051 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0A1986BD29CF6FE4	FASTA	63	7,228
	10 20 30 40 50 60 MTKQEKTALN MARFIRSQTL TLLEKLNELD ADEQADICES LHDHADELYR SCLARFGDDG ENL

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.

PIR

RGECRE. A03587.

RefSeq

NP_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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B6Q	X-ray	1.80	A	1-63	[»]
1F4M	X-ray	2.25	A/B/C/D/E/F	2-63	[»]
1F4N	X-ray	1.90	A/B	2-63	[»]
1GMG	X-ray	1.90	A/B	1-63	[»]
1GTO	X-ray	1.82	A/B/C	2-62	[»]
1NKD	X-ray	1.09	A	1-63	[»]
1QX8	X-ray	2.02	A/B	1-63	[»]
1ROP	X-ray	1.70	A	1-63	[»]
1RPO	X-ray	1.40	A	1-63	[»]
1RPR	NMR	-	A/B	1-63	[»]
1YO7	X-ray	2.80	A/B	1-56	[»]
2GHY	X-ray	2.50	A/B	1-63	[»]
2IJH	X-ray	1.80	A/B/C	2-63	[»]
2IJI	X-ray	2.30	A	2-63	[»]
2IJJ	X-ray	1.90	A/B/C	2-63	[»]
2IJK	X-ray	1.55	A/B	2-63	[»]
3K79	X-ray	1.96	A	2-63	[»]
4DO2	X-ray	1.40	A/B	1-63	[»]

ProteinModelPortal

P03051.

SMR

P03051. Positions 1-63.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48900N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

13877151.
13906508.
14401266.
1446623.
2693963.
4397513.

Phylogenomic databases

ProtClustDB

CLSK861667.

Family and domain databases

InterPro

IPR000769. Regulatory_Rop.
[Graphical view]

Pfam

PF01815. Rop. 1 hit.
[Graphical view]

PIRSF

PIRSF003229. Rop_reg. 1 hit.

PRINTS

PR00835. ROPREGULATRY.

ProDom

PD012167. Rop_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF47380. Rop_reg. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P03051.

Entry information

Entry name

ROP_ECOLX

Accession

Primary (citable) accession number: P03051

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program