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Protein

Major capsid protein

Gene

5

Organism
Salmonella phage P22 (Bacteriophage P22)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Assembles to form an icosahedral capsid with a T=7 symmetry.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei14Essential for binding to the capsid assembly scaffolding protein1 Publication1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: CAFA

GO - Biological processi

  • viral procapsid maturation Source: CAFA

Names & Taxonomyi

Protein namesi
Recommended name:
Major capsid proteinCurated
Alternative name(s):
Gene product 5Curated
Short name:
gp5
Major head proteinCurated
Gene namesi
Name:5
OrganismiSalmonella phage P22 (Bacteriophage P22)
Taxonomic identifieri10754 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeP22virus
Virus hostiSalmonella typhimurium [TaxID: 90371]
Proteomesi
  • UP000002165 Componenti: Genome
  • UP000001795 Componenti: Genome
  • UP000001796 Componenti: Genome
  • UP000007960 Componenti: Genome
  • UP000001315 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • T=7 icosahedral viral capsid Source: UniProtKB-KW
  • viral capsid Source: CAFA
  • viral procapsid Source: CAFA

Keywords - Cellular componenti

Capsid protein, T=7 icosahedral capsid protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5E → A: Impaired phage growth; probable capsid protein misfolding. 1 Publication1
Mutagenesisi14D → A: Impaired phage growth; inability of the mutant capsid protein to interact properly with scaffolding protein. 1 Publication1
Mutagenesisi15E → A: Decreased phage growth. 1 Publication1
Mutagenesisi18E → A: Decreased phage growth. 1 Publication1
Mutagenesisi241W → A: Cold-sensitive phnotype probably due to an assembly defect. 1 Publication1
Mutagenesisi242Q → A: Cold-sensitive phnotype probably due to an assembly defect. 1 Publication1
Mutagenesisi243L → A: No effect on phage production. 1 Publication1
Mutagenesisi244D → A: Lethal. Complete loss of procapsids assembly. 1 Publication1
Mutagenesisi245N → A: Slight decrease in phage production. 1 Publication1
Mutagenesisi246D → A: Lethal. Complete loss of procapsids assembly, assembles as tubes instead. 1 Publication1
Mutagenesisi249K → A: No effect on phage production. 1 Publication1
Mutagenesisi251N → A: Cold-sensitive phnotype probably due to an assembly defect. 1 Publication1
Mutagenesisi377K → A: No effect on phage growth. 1 Publication1
Mutagenesisi385D → A: No effect on phage growth. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by host1 Publication
ChainiPRO_00000777522 – 430Major capsid proteinAdd BLAST429

Proteomic databases

PRIDEiP26747

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts (via N-terminus) with the capsid assembly scaffolding protein (via C-terminus); capsid proteins and scaffolding proteins form building blocks that assemble to form the procapsid.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-15582363,EBI-15582363

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: CAFA

Protein-protein interaction databases

DIPiDIP-29111N
IntActiP26747, 1 interactor

Structurei

Secondary structure

1430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 29Combined sources4
Beta strandi30 – 33Combined sources4
Helixi37 – 42Combined sources6
Beta strandi45 – 50Combined sources6
Beta strandi74 – 78Combined sources5
Beta strandi83 – 90Combined sources8
Helixi91 – 94Combined sources4
Helixi99 – 125Combined sources27
Beta strandi128 – 135Combined sources8
Turni140 – 142Combined sources3
Helixi143 – 157Combined sources15
Beta strandi166 – 170Combined sources5
Helixi172 – 182Combined sources11
Helixi183 – 185Combined sources3
Helixi193 – 196Combined sources4
Turni197 – 199Combined sources3
Beta strandi200 – 204Combined sources5
Helixi205 – 207Combined sources3
Beta strandi210 – 213Combined sources4
Beta strandi228 – 232Combined sources5
Beta strandi240 – 243Combined sources4
Beta strandi249 – 251Combined sources3
Beta strandi253 – 255Combined sources3
Beta strandi257 – 262Combined sources6
Beta strandi272 – 281Combined sources10
Beta strandi283 – 285Combined sources3
Beta strandi288 – 297Combined sources10
Beta strandi302 – 310Combined sources9
Beta strandi313 – 316Combined sources4
Turni322 – 324Combined sources3
Helixi325 – 327Combined sources3
Beta strandi330 – 332Combined sources3
Beta strandi336 – 342Combined sources7
Beta strandi351 – 355Combined sources5
Beta strandi359 – 363Combined sources5
Helixi371 – 373Combined sources3
Beta strandi376 – 382Combined sources7
Turni384 – 386Combined sources3
Beta strandi389 – 397Combined sources9
Turni398 – 401Combined sources4
Beta strandi402 – 409Combined sources8
Beta strandi411 – 416Combined sources6
Turni418 – 420Combined sources3
Beta strandi421 – 426Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M5SNMR-A223-345[»]
2XYYelectron microscopy3.80A/B/C/D/E/F/G1-430[»]
2XYZelectron microscopy4.00A/B/C/D/E/F/G1-430[»]
3IYHelectron microscopy-A/B/C/D/E/F1-430[»]
3IYIelectron microscopy-A/B/C/D/E/F/G1-430[»]
5UU5electron microscopy3.30A/B/C/D/E/F/G1-430[»]
SMRiP26747
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26747

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 56Binding to the capsid assembly scaffolding protein1 PublicationAdd BLAST55
Regioni223 – 345I domain1 PublicationAdd BLAST123

Domaini

The insertion domain (I domain) plays an important role in the folding of the capsid protein by acting as an intramolecular chaperone.2 Publications

Sequence similaritiesi

Phylogenomic databases

OrthoDBiVOG0900009D

Family and domain databases

InterProiView protein in InterPro
IPR024659 Phage_coat_Gp5
PfamiView protein in Pfam
PF11651 P22_CoatProtein, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26747-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALNEGQIVT LAVDEIIETI SAITPMAQKA KKYTPPAASM QRSSNTIWMP
60 70 80 90 100
VEQESPTQEG WDLTDKATGL LELNVAVNMG EPDNDFFQLR ADDLRDETAY
110 120 130 140 150
RRRIQSAARK LANNVELKVA NMAAEMGSLV ITSPDAIGTN TADAWNFVAD
160 170 180 190 200
AEEIMFSREL NRDMGTSYFF NPQDYKKAGY DLTKRDIFGR IPEEAYRDGT
210 220 230 240 250
IQRQVAGFDD VLRSPKLPVL TKSTATGITV SGAQSFKPVA WQLDNDGNKV
260 270 280 290 300
NVDNRFATVT LSATTGMKRG DKISFAGVKF LGQMAKNVLA QDATFSVVRV
310 320 330 340 350
VDGTHVEITP KPVALDDVSL SPEQRAYANV NTSLADAMAV NILNVKDART
360 370 380 390 400
NVFWADDAIR IVSQPIPANH ELFAGMKTTS FSIPDVGLNG IFATQGDIST
410 420 430
LSGLCRIALW YGVNATRPEA IGVGLPGQTA
Length:430
Mass (Da):46,752
Last modified:January 23, 2007 - v2
Checksum:iBBDF63575C4B3899
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59749 Genomic DNA Translation: AAA72963.1
AF217253 Genomic DNA Translation: AAF75047.1
BK000583 Genomic DNA Translation: DAA00987.1
AF527608 Genomic DNA Translation: AAM81389.1
AB362338 Genomic DNA Translation: BAF80720.1
AB426868 Genomic DNA Translation: BAG12603.1
PIRiE40474 Z5BP22
RefSeqiNP_059630.1, NC_002371.2

Genome annotation databases

GeneIDi1262831
KEGGivg:1262831

Similar proteinsi

Entry informationi

Entry nameiCAPSD_BPP22
AccessioniPrimary (citable) accession number: P26747
Secondary accession number(s): A8CGC7, Q77D91, Q7PCI5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 78 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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