P03641 (F_BPPHX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Capsid protein F

Alternative name(s):
F protein
GPF

Gene names

Name:

F

Organism

Enterobacteria phage phiX174 (Bacteriophage phi-X174)

Taxonomic identifier

10847 [NCBI]

Taxonomic lineage

Viruses › ssDNA viruses › Microviridae › Microvirus

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	427 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	Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F. Ref.5
Subunit structure	Pentamerizes and interacts with H protein, G and B pentamers to form 12S pre-assembly complex. By binding with protein D, induces joining of twelve 12S complex to form the procapsid. Upon genome packaging, interacts with protein J. Ref.8
Subcellular location	Virion. Host cytoplasm.
Sequence similarities	Belongs to the microviridae F protein family.

Ontologies

Keywords
Cellular component	Host cytoplasm Virion
Molecular function	Capsid protein T=1 icosahedral capsid protein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 Ref.3

Chain

2 – 427

426

Capsid protein F

PRO_0000164890

Secondary structure

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427

Helix Strand Turn

Details...

Beta strand

11 – 14

4

Beta strand

17 – 23

7

Beta strand

25 – 36

12

Beta strand

41 – 52

12

Beta strand

55 – 58

4

Beta strand

63 – 73

11

Helix

74 – 88

15

Helix

89 – 91

3

Beta strand

97 – 99

3

Turn

104 – 107

4

Helix

108 – 110

3

Beta strand

119 – 121

3

Helix

122 – 135

14

Helix

149 – 151

3

Helix

154 – 159

6

Turn

169 – 171

3

Helix

193 – 211

19

Helix

216 – 222

7

Turn

229 – 233

5

Beta strand

236 – 245

10

Beta strand

248 – 251

4

Turn

255 – 259

5

Beta strand

261 – 264

4

Beta strand

266 – 277

12

Beta strand

280 – 291

12

Beta strand

296 – 299

4

Helix

302 – 305

4

Beta strand

306 – 308

3

Helix

311 – 314

4

Helix

318 – 321

4

Beta strand

327 – 330

4

Helix

331 – 333

3

Beta strand

343 – 346

4

Helix

350 – 352

3

Helix

361 – 363

3

Helix

380 – 384

5

Helix

388 – 394

7

Beta strand

402 – 415

14

Helix

420 – 424

5

Sequences

	Sequence		Length	Mass (Da)
	P03641 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 837DE99C73F426BC	FASTA	427	48,483
	10 20 30 40 50 60 MSNIQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL RLSPLRRGLA 70 80 90 100 110 120 IDSTVDIFTF YVPHRHVYGE QWIKFMKDGV NATPLPTVNT TGYIDHAAFL GTINPDTNKI 130 140 150 160 170 180 PKHLFQGYLN IYNNYFKAPW MPDRTEANPN ELNQDDARYG FRCCHLKNIW TAPLPPETEL 190 200 210 220 230 240 SRQMTTSTTS IDIMGLQAAY ANLHTDQERD YFMQRYHDVI SSFGGKTSYD ADNRPLLVMR 250 260 270 280 290 300 SNLWASGYDV DGTDQTSLGQ FSGRVQQTYK HSVPRFFVPE HGTMFTLALV RFPPTATKEI 310 320 330 340 350 360 QYLNAKGALT YTDIAGDPVL YGNLPPREIS MKDVFRSGDS SKKFKIAEGQ WYRYAPSYVS 370 380 390 400 410 420 PAYHLLEGFP FIQEPPSGDL QERVLIRHHD YDQCFQSVQL LQWNSQVKFN VTVYRNLPTT RDSIMTS

References

[1]	"Nucleotide sequence of bacteriophage phi X174 DNA." Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C., Hutchison C.A. III, Slocombe P.M., Smith M. Nature 265:687-695(1977) [PubMed: 870828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of bacteriophage phiX174." Sanger F., Coulson A.R., Friedmann T., Air G.M., Barrell B.G., Brown N.L., Fiddes J.C., Hutchison C.A. III, Slocombe P.M., Smith M. J. Mol. Biol. 125:225-246(1978) [PubMed: 731693] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"Amino acid sequences from the gene F (capsid) protein of bacteriophage phiX174." Air G.M. J. Mol. Biol. 107:433-443(1976) [PubMed: 794486] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-95.
[4]	"Nucleotide sequence of the F protein coding region of bacteriophage phiX174 and the amino acid sequence of its product." Air G.M., Coulson A.R., Fiddes J.C., Friedmann T., Hutchison C.A. III, Sanger F., Slocombe P.M., Smith A.J.H. J. Mol. Biol. 125:247-254(1978) [PubMed: 731694] [Abstract] Cited for: PROTEIN SEQUENCE OF 86-427.
[5]	"phi X174 genome-capsid interactions influence the biophysical properties of the virion: evidence for a scaffolding-like function for the genome during the final stages of morphogenesis." Hafenstein S., Fane B.A. J. Virol. 76:5350-5356(2002) [PubMed: 11991963] [Abstract] Cited for: FUNCTION.
[6]	"Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications." McKenna R., Xia D., Williangmann P., Ilag L.L., Krishnaswamy S., Rossmann M.G., Olson N.H., Baker T.S., Incardona N.L. Nature 355:137-143(1992) [PubMed: 1370343] [Abstract] Cited for: CRYSTALLIZATION.
[7]	"Analysis of the single-stranded DNA bacteriophage phi X174, refined at a resolution of 3.0 A." McKenna R., Ilag L.L., Rossmann M.G. J. Mol. Biol. 237:517-543(1994) [PubMed: 8158636] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[8]	"Structure of a viral procapsid with molecular scaffolding." Dokland T., McKenna R., Ilag L.L., Bowman B.R., Incardona N.L., Fane B.A., Rossmann M.G. Nature 389:308-313(1997) [PubMed: 9305849] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), INTERACTION WITH J PROTEIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02482 Genomic DNA. Translation: AAA32578.1.

PIR

ZFBPF4. B93185.

RefSeq

NP_040711.1. NC_001422.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AL0	X-ray	3.50	F	2-427	[»]
1CD3	X-ray	3.50	F	2-426	[»]
1KVP	electron microscopy	27.00	A	2-427	[»]
1PHX	model	-	1	1-427	[»]
2BPA	X-ray	3.00	1	2-427	[»]

ProteinModelPortal

P03641.

SMR

P03641. Positions 2-427.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6198N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2546408.

GenomeReviews

Gene locus phiX174p10 in contig J02482_GR.

Phylogenomic databases

ProtClustDB

PHA0009.

Family and domain databases

InterPro

IPR016184. Capsid/spike_ssDNA_virus.
IPR003514. Capsid_protein_F.
[Graphical view]

Gene3D

G3DSA:2.60.169.10. Caspid_F. 1 hit.

Pfam

PF02305. Phage_F. 2 hits.
[Graphical view]

SUPFAM

SSF88645. Capsid/spike_ssDNA_virus. 1 hit.

ProtoNet

Search...

Entry information

Entry name

F_BPPHX

Accession

Primary (citable) accession number: P03641

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program