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Protein

Major capsid protein

Gene

gp23

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Major capsid protein that self-associates to form hexamers, building most of the capsid in association with pentons made of the capsid vertex protein and one dodecamer of the portal protein. The major capsid protein self-associates to form 160 hexamers, building most of the T=13 laevo capsid. Folding of major capsid protein requires the assistance of two chaperones, the host chaperone groL acting with the phage encoded gp23-specific chaperone, gp31. The capsid also contains two nonessential outer capsid proteins, Hoc and Soc, which decorate the capsid surface. Through binding to adjacent gp23 subunits, Soc reinforces the capsid structure.UniRule annotation4 Publications

Names & Taxonomyi

Protein namesi
Recommended name:
Major capsid protein1 PublicationUniRule annotation
Alternative name(s):
Gene product 231 Publication
Major head proteinUniRule annotationCurated
gp231 PublicationUniRule annotation
Cleaved into the following chain:
Mature major capsid proteinUniRule annotationCurated
Alternative name(s):
gp23*1 PublicationUniRule annotation
Gene namesi
Name:gp23
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4virus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000009087 Componenti: Genome

Subcellular locationi

Major capsid protein :
  • Virion
  • Note: Part of the capsid icosahedric shell of the immature virion. The capsid is made of 930 copies arranged as 160 hexamers.UniRule annotation2 Publications
Mature major capsid protein :

GO - Cellular componenti

  • T=13 icosahedral viral capsid Source: UniProtKB-KW
  • viral capsid Source: CACAO
  • virion Source: CACAO

Keywords - Cellular componenti

Capsid protein, T=13 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001649211 – 521Major capsid proteinAdd BLAST521
ChainiPRO_000043019666 – 521Mature major capsid protein1 PublicationAdd BLAST456

Post-translational modificationi

A proteolytic cleavage gives rise to the mature major capsid protein during virus maturation.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei65 – 66CleavageUniRule annotation1 Publication2

Proteomic databases

PRIDEiP04535

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Homohexamer. Interacts with the portal protein. Interacts with the capsid vertex protein that forms pentamers. Interacts with hoc; one hoc molecule associates with each capsid hexamer. Interacts with soc; this interaction reinforces the capsid structure. A total of 960 subunits of the major capsid protein forms the 160 hexamers.UniRule annotation4 Publications

Protein-protein interaction databases

DIPiDIP-59725N
IntActiP04535, 2 interactors

Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi76 – 81Combined sources6
Beta strandi85 – 87Combined sources3
Beta strandi98 – 100Combined sources3
Beta strandi118 – 121Combined sources4
Beta strandi123 – 127Combined sources5
Beta strandi129 – 133Combined sources5
Beta strandi135 – 137Combined sources3
Beta strandi142 – 144Combined sources3
Beta strandi146 – 148Combined sources3
Beta strandi152 – 156Combined sources5
Helixi157 – 160Combined sources4
Beta strandi177 – 181Combined sources5
Beta strandi183 – 185Combined sources3
Beta strandi187 – 194Combined sources8
Helixi205 – 217Combined sources13
Beta strandi220 – 224Combined sources5
Helixi230 – 234Combined sources5
Beta strandi237 – 239Combined sources3
Beta strandi249 – 252Combined sources4
Beta strandi255 – 258Combined sources4
Beta strandi263 – 267Combined sources5
Helixi272 – 282Combined sources11
Helixi290 – 313Combined sources24
Beta strandi314 – 318Combined sources5
Helixi320 – 322Combined sources3
Beta strandi329 – 333Combined sources5
Turni337 – 342Combined sources6
Helixi347 – 367Combined sources21
Beta strandi375 – 378Combined sources4
Helixi380 – 387Combined sources8
Beta strandi407 – 410Combined sources4
Beta strandi412 – 417Combined sources6
Turni418 – 420Combined sources3
Beta strandi421 – 425Combined sources5
Beta strandi434 – 436Combined sources3
Beta strandi446 – 450Combined sources5
Beta strandi453 – 462Combined sources10
Turni464 – 466Combined sources3
Beta strandi469 – 476Combined sources8
Beta strandi479 – 481Combined sources3
Beta strandi493 – 498Combined sources6
Helixi503 – 506Combined sources4
Beta strandi510 – 519Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z1Umodel-A/B/C/D/E/F74-521[»]
5VF3electron microscopy3.30A/B/C/D/E/F/G/H/I/J/K/L66-521[»]
SMRiP04535
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Tevenvirinae major capsid protein family.UniRule annotation

Phylogenomic databases

KOiK21079
OrthoDBiVOG0900006G

Family and domain databases

HAMAPiMF_04117 CAPSID_H_T4, 1 hit
InterProiView protein in InterPro
IPR038997 CAPSID_Myoviridae
IPR010762 Gp23/Gp24_T4-like
PfamiView protein in Pfam
PF07068 Gp23, 1 hit

Sequencei

Sequence statusi: Complete.

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

P04535-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIKTKAELL NKWKPLLEGE GLPEIANSKQ AIIAKIFENQ EKDFQTAPEY
60 70 80 90 100
KDEKIAQAFG SFLTEAEIGG DHGYNATNIA AGQTSGAVTQ IGPAVMGMVR
110 120 130 140 150
RAIPNLIAFD ICGVQPMNSP TGQVFALRAV YGKDPVAAGA KEAFHPMYGP
160 170 180 190 200
DAMFSGQGAA KKFPALAAST QTTVGDIYTH FFQETGTVYL QASVQVTIDA
210 220 230 240 250
GATDAAKLDA EIKKQMEAGA LVEIAEGMAT SIAELQEGFN GSTDNPWNEM
260 270 280 290 300
GFRIDKQVIE AKSRQLKAAY SIELAQDLRA VHGMDADAEL SGILATEIML
310 320 330 340 350
EINREVVDWI NYSAQVGKSG MTLTPGSKAG VFDFQDPIDI RGARWAGESF
360 370 380 390 400
KALLFQIDKE AVEIARQTGR GEGNFIIASR NVVNVLASVD TGISYAAQGL
410 420 430 440 450
ATGFSTDTTK SVFAGVLGGK YRVYIDQYAK QDYFTVGYKG PNEMDAGIYY
460 470 480 490 500
APYVALTPLR GSDPKNFQPV MGFKTRYGIG INPFAESAAQ APASRIQSGM
510 520
PSILNSLGKN AYFRRVYVKG I
Length:521
Mass (Da):56,022
Last modified:December 19, 2001 - v2
Checksum:i41E495E66D96A453
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti311N → D AA sequence (PubMed:3447164).Curated1
Sequence conflicti405S → N in AAA32503 (PubMed:6335532).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01774 Genomic DNA Translation: CAA25911.1
K01765 Genomic DNA Translation: AAA32503.1
AF158101 Genomic DNA Translation: AAD42428.1
PIRiA92911 VHBPT4
RefSeqiNP_049787.1, NC_000866.4

Genome annotation databases

GeneIDi1258751
KEGGivg:1258751

Similar proteinsi

Entry informationi

Entry nameiCAPSH_BPT4
AccessioniPrimary (citable) accession number: P04535
Secondary accession number(s): Q94N06
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 19, 2001
Last modified: May 23, 2018
This is version 84 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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