Annotation for this protein is in progress - please check future releases for more complete information


DP00268: Coat proteinFASTA viewXML view

General information
DisProt:DP00268
Name:Coat protein
Synonym(s):VG05_BPP22
Protein gp5
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P26747
UniGene: 
SwissProt: VG05_BPP22
TrEMBL:  
NCBI (GI): 137894
Source organism:Enterobacteria phage P22 (Bacteriophage P22)
Sequence length:430
Percent disordered:44%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MALNEGQIVT LAVDEIIETI SAITPMAQKA KKYTPPAASM QRSSNTIWMP VEQESPTQEG - 60
WDLTDKATGL LELNVAVNMG EPDNDFFQLR ADDLRDETAY RRRIQSAARK LANNVELKVA - 120
NMAAEMGSLV ITSPDAIGTN TADAWNFVAD AEEIMFSREL NRDMGTSYFF NPQDYKKAGY - 180
DLTKRDIFGR IPEEAYRDGT IQRQVAGFDD VLRSPKLPVL TKSTATGITV SGAQSFKPVA - 240
WQLDNDGNKV NVDNRFATVT LSATTGMKRG DKISFAGVKF LGQMAKNVLA QDATFSVVRV - 300
VDGTHVEITP KPVALDDVSL SPEQRAYANV NTSLADAMAV NILNVKDART NVFWADDAIR - 360
IVSQPIPANH ELFAGMKTTS FSIPDVGLNG IFATQGDIST LSGLCRIALW YGVNATRPEA - 420
IGVGLPGQTA



Functional narrative    

Function: Required for successful condensation of DNA within the capsid. Gp5 is the major structural protein of the outer shell of the prohead.
Subunit structure: Present in about 400 copies as an icosahedrally symmetric matrix.
Subcellular location: Virion (potential).
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Region 1: 2-191

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:N-terminal domain
Location:2 - 191
Length:190
Region sequence:

ALNEGQIVTLAVDEIIETISAITPMAQKAKKYTPPAASMQRSSNTIWMPVEQESPTQEGW
DLTDKATGLLELNVAVNMGEPDNDFFQLRADDLRDETAYRRRIQSAARKLANNVELKVAN
MAAEMGSLVITSPDAIGTNTADAWNFVADAEEIMFSRELNRDMGTSYFFNPQDYKKAGYD
LTKRDIFGRI

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to molten globule transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, near-UV (293 K; NaCl (pH 7.6) 25 mM; PO4 25 mM)

  2. Hydrogen-deuterium exchange (294 K; pH: 7.6; 2H2O 90 %)
References:
  1. Kang S, Prevelige PE Jr. "Domain study of bacteriophage p22 coat protein and characterization of the capsid lattice transformation by hydrogen/deuterium exchange." J Mol Biol. 2005; 347(5): 935-48. PubMed: 15784254
Comments:
The N-terminal domain adopts additional structure in the context of the C-terminal domain but retains some flexibility.


Comments


PDB electron microscope structures for this protein: 3IYH and 3IYI. Parent et al (2010), PMID 20223221.


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