P03612 (COAT_BPMS2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Coat protein
Organism	Enterobacteria phage MS2 (Bacteriophage MS2) [Reference proteome]
Taxonomic identifier	329852 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Leviviridae › Levivirus
Virus host	Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	130 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Forms the phage shell; binds to the phage RNA.
Subunit structure	The shell is composed of 180 copies of the coat protein. The coat protein form dimers that assemble by group of 5. Twelve such pentamers are linked together with free dimers.
Subcellular location	Virion Potential.

Ontologies

Keywords
Cellular component	Virion
Ligand	RNA-binding
Molecular function	Capsid protein T=3 icosahedral capsid protein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	T=3 icosahedral viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed; by host

Chain

2 – 130

129

Coat protein

PRO_0000164843

Secondary structure

1

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130

Helix Strand Turn

Details...

Beta strand

8 – 11

4

Beta strand

13 – 17

5

Beta strand

19 – 27

9

Beta strand

30 – 34

5

Beta strand

38 – 40

3

Beta strand

44 – 53

10

Beta strand

56 – 65

10

Beta strand

70 – 75

6

Beta strand

79 – 83

5

Beta strand

85 – 94

10

Beta strand

95 – 97

3

Helix

99 – 112

14

Helix

118 – 125

8

Beta strand

126 – 129

4

Sequences

	Sequence		Length	Mass (Da)
	P03612 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: ABCDD9FD8B188C6A	FASTA	130	13,860
	10 20 30 40 50 60 MASNFTQFVL VDNGGTGDVT VAPSNFANGV AEWISSNSRS QAYKVTCSVR QSSAQNRKYT 70 80 90 100 110 120 IKVEVPKVAT QTVGGVELPV AAWRSYLNME LTIPIFATNS DCELIVKAMQ GLLKDGNPIP 130 SAIAANSGIY

References

[1]	"Nucleotide sequence of the gene coding for the bacteriophage MS2 coat protein." Min Jou W., Haegeman G., Ysebaert M., Fiers W. Nature 237:82-88(1972) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The three-dimensional structure of the bacterial virus MS2." Valegaard K., Liljas L., Fridborg K., Unge T. Nature 345:36-41(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
[3]	"Structure determination of the bacteriophage MS2." Valegard K., Liljas L., Fridborg K., Unge T. Acta Crystallogr. B 47:949-960(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
[4]	"The refined structure of bacteriophage MS2 at 2.8-A resolution." Golmohammadi R., Valegaard K., Fridborg K., Liljas L. J. Mol. Biol. 234:620-639(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[5]	"Crystal structure of an RNA bacteriophage coat protein-operator complex." Valegaard K., Murray J.B., Sotckley P.G., Stonehouse N.J., Liljas L. Nature 371:623-626(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[6]	"Crystal structures of MS2 capsids with mutations in the subunit FG loop." Stonehouse N.J., Valegaard K., Golmohammadi R., van den Worm S., Walton C., Stockley P.G., Liljas L. J. Mol. Biol. 256:330-339(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[7]	"Crystal structure of an RNA aptamer-protein complex at 2.8-A resolution." Convery M.A., Rowsell S., Stonehouse N.J., Ellington A.D., Hirao I., Murray J.B., Peabody D.S., Phillips S.E.V., Stockley P.G. Nat. Struct. Biol. 5:133-139(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH RNA.
[8]	"Crystal structures of a series of RNA aptamers complexed to the same protein target." Rowsell S., Stonehouse N.J., Convery M.A., Adams C.J., Ellington A.D., Hirao I., Peabody D.S., Stockley P.G., Phillips S.E. Nat. Struct. Biol. 5:970-975(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure assembled from a chemically modified RNA genome hairpin variant

Virus Particle ExploreR db

Icosahedral capsid structure assembled from a modified RNA genome hairpin variant G7

Virus Particle ExploreR db

Icosahedral capsid structure assembled from modified RNA genome hairpin variant G10

Virus Particle ExploreR db

Icosahedral capsid structure assembled from modified RNA genome hairpin variant C10

Virus Particle ExploreR db

Icosahedral capsid structure of mutant E77D

Virus Particle ExploreR db

Icosahedral capsid structure of mutant T60S

Virus Particle ExploreR db

Icosahedral capsid structure of mutant T46A

Virus Particle ExploreR db

Icosahedral capsid structure of mutant T46A

Virus Particle ExploreR db

Icosahedral capsid structure of mutant T60S

Virus Particle ExploreR db

Icosahedral capsid structure of mutant P79N

Virus Particle ExploreR db

Icosahedral capsid structure associated with 8 nt RNA

Virus Particle ExploreR db

Icosahedral capsid structure associated with 19 nt RNA

Virus Particle ExploreR db

Icosahedral capsid structure associated with 19 nt RNA

Virus Particle ExploreR db

Icosahedral capsid structure associated with 23 nt RNA

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure associated with a aptamer RNA

Virus Particle ExploreR db

Icosahedral capsid structure associated with a F5 aptamer RNA

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00642 mRNA. Translation: CAA23989.1.

PIR

VCBPM2. B04222.

RefSeq

NP_040648.1. NC_001417.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AQ3	X-ray	2.80	A/B/C	2-129	[»]
1AQ4	X-ray	3.00	A/B/C	2-129	[»]
1BMS	X-ray	2.70	A/B/C	2-130	[»]
1MSC	X-ray	2.00	A	2-129	[»]
1MST	X-ray	2.60	A/B/C	2-130	[»]
1MVA	X-ray	3.00	A/B/C	2-129	[»]
1MVB	X-ray	3.00	A/B/C	2-129	[»]
1U1Y	X-ray	2.85	A/B/C	2-129	[»]
1ZDH	X-ray	2.70	A/B/C	2-129	[»]
1ZDI	X-ray	2.70	A/B/C	2-130	[»]
1ZDJ	X-ray	2.90	A/B/C	2-129	[»]
1ZDK	X-ray	2.86	A/B/C	2-129	[»]
1ZSE	X-ray	3.00	A/B/C	2-129	[»]
2B2D	X-ray	2.90	A/B/C	2-130	[»]
2B2E	X-ray	3.15	A/B/C	2-129	[»]
2B2G	X-ray	3.02	A/B/C	2-129	[»]
2BNY	X-ray	3.00	A/B/C	2-129	[»]
2BQ5	X-ray	2.91	A/B/C	2-129	[»]
2BS0	X-ray	2.45	A/B/C	2-129	[»]
2BS1	X-ray	2.80	A/B/C	2-130	[»]
2BU1	X-ray	2.20	A/B/C	2-129	[»]
2C4Q	X-ray	2.38	A/B/C	2-130	[»]
2C4Y	X-ray	2.68	A/B/C	2-129	[»]
2C4Z	X-ray	2.60	A/B/C	2-129	[»]
2C50	X-ray	2.65	A/B/C	2-129	[»]
2C51	X-ray	2.80	A/B/C	2-129	[»]
2IZ8	X-ray	3.30	A/B/C	2-129	[»]
2IZ9	X-ray	2.85	A/B/C	2-129	[»]
2IZM	X-ray	2.70	A/B/C	2-129	[»]
2IZN	X-ray	2.56	A/B/C	2-129	[»]
2MS2	X-ray	2.80	A/B/C	2-130	[»]
2VTU	X-ray	3.50	J/L	2-130	[»]
2WBH	X-ray	4.70	A/B/C	2-130	[»]
5MSF	X-ray	2.80	A/B/C	2-130	[»]
6MSF	X-ray	2.80	A/B/C	2-130	[»]
7MSF	X-ray	2.80	A/B/C	2-130	[»]

ProteinModelPortal

P03612.

SMR

P03612. Positions 2-130.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1260899.

Phylogenomic databases

ProtClustDB

PHA0026.

Family and domain databases

Gene3D

3.30.380.10. 1 hit.

InterPro

IPR002703. Phage_MS2_coat.
IPR015954. Phage_RNA-type_capsid.
[Graphical view]

Pfam

PF01819. Levi_coat. 1 hit.
[Graphical view]

SUPFAM

SSF55405. Levi_coat. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P03612.

Entry information

Entry name

COAT_BPMS2

Accession

Primary (citable) accession number: P03612

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program