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Protein

Baseplate central spike complex protein gp5

Gene

5

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

Functioni

Baseplate central spike complex-associated lysozyme that is essential for the localized hydrolysis of bacterial cell wall in the periplasmic space, a necessary step for viral DNA ejection into the host cell. Involved in the tail assembly.1 Publication1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.1 Publication

pH dependencei

Optimum pH is 5.8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei184Proton donorBy similarity1
Active sitei193NucleophileBy similarity1

GO - Molecular functioni

  • identical protein binding Source: CAFA
  • lysozyme activity Source: UniProtKB
  • peptidoglycan beta-N-acetylmuramidase activity Source: CACAO

GO - Biological processi

  • cell wall macromolecule catabolic process Source: InterPro
  • cytolysis Source: UniProtKB-KW
  • defense response to bacterium Source: UniProtKB-KW
  • disruption by virus of host cell wall peptidoglycan during virus entry Source: UniProtKB-KW
  • entry into host via enzymatic degradation of host anatomical structure Source: UniProtKB
  • pathogenesis Source: CAFA
  • peptidoglycan catabolic process Source: InterPro
  • protein homotrimerization Source: CAFA
  • viral tail assembly Source: UniProtKB-KW

Keywordsi

Molecular functionAntimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase
Biological processDegradation of host cell envelope components during virus entry, Degradation of host peptidoglycans during virus entry, Viral genome ejection through host cell envelope, Viral penetration into host cytoplasm, Viral release from host cell, Viral tail assembly, Virus entry into host cell

Protein family/group databases

CAZyiGH24 Glycoside Hydrolase Family 24
TCDBi1.K.1.1.1 the gp27/5 t4-baseplate (t4-bp) family

Names & Taxonomyi

Protein namesi
Recommended name:
Baseplate central spike complex protein gp51 Publication
Alternative name(s):
Peptidoglycan hydrolase gp5 (EC:3.2.1.171 Publication)
Protein Gp5
Cleaved into the following 2 chains:
Gene namesi
Name:5
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

GO - Cellular componenti

  • virion Source: CACAO
  • virus tail Source: CAFA
  • virus tail, baseplate Source: UniProtKB

Keywords - Cellular componenti

Viral baseplate protein, Viral tail protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002181111 – 575Baseplate central spike complex protein gp5Add BLAST575
ChainiPRO_00004083601 – 351Gp5*1 PublicationAdd BLAST351
ChainiPRO_0000408361352 – 575Gp5C1 PublicationAdd BLAST224

Post-translational modificationi

In the fully assembled virus, gp5 is cleaved after residue 351, but the resulting fragments, gp5* and gp5C, remain associated with the virion.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei351 – 352Cleavage2

Proteomic databases

PRIDEiP16009

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Homotrimer (PubMed:12837775, PubMed:19896486, PubMed:11823865). Heteromultimer with gp27 trimer and gp5.4 monomer; this interaction forms the central spike complex that creates an extension of the tail tube (PubMed:12837775, PubMed:27193680). The central spike complex is made up of three copies of the gp27-gp5*-gp5C complex and one copy of gp5.4 (PubMed:11823865, PubMed:27193680). Part of the baseplate macromolecular complex which consists of gp5, gp5.4, gp27 (central spike complex); gp6, gp25, gp53 (inner baseplate); gp7, gp8 (intermediate baseplate); gp9, gp10, gp11, gp12 (peripheral); gp48 and gp54 (proximal region of the tail tube) (PubMed:27193680).1 Publication4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
27P171722EBI-1032754,EBI-1032762

GO - Molecular functioni

  • identical protein binding Source: CAFA

Protein-protein interaction databases

IntActiP16009, 1 interactor
MINTiP16009

Structurei

Secondary structure

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 17Combined sources9
Beta strandi27 – 31Combined sources5
Turni32 – 34Combined sources3
Beta strandi43 – 45Combined sources3
Helixi49 – 51Combined sources3
Beta strandi54 – 57Combined sources4
Beta strandi69 – 71Combined sources3
Beta strandi81 – 86Combined sources6
Beta strandi94 – 99Combined sources6
Beta strandi103 – 106Combined sources4
Beta strandi112 – 115Combined sources4
Beta strandi117 – 119Combined sources3
Beta strandi124 – 129Combined sources6
Helixi131 – 134Combined sources4
Helixi136 – 140Combined sources5
Helixi143 – 149Combined sources7
Beta strandi154 – 156Combined sources3
Turni163 – 165Combined sources3
Helixi176 – 184Combined sources9
Beta strandi187 – 192Combined sources6
Beta strandi194 – 196Combined sources3
Beta strandi198 – 201Combined sources4
Beta strandi204 – 206Combined sources3
Helixi214 – 225Combined sources12
Turni231 – 234Combined sources4
Helixi238 – 257Combined sources20
Helixi262 – 268Combined sources7
Helixi271 – 284Combined sources14
Helixi286 – 290Combined sources5
Helixi293 – 300Combined sources8
Helixi304 – 311Combined sources8
Helixi315 – 318Combined sources4
Turni319 – 322Combined sources4
Helixi323 – 333Combined sources11
Beta strandi334 – 336Combined sources3
Helixi337 – 339Combined sources3
Beta strandi347 – 350Combined sources4
Turni354 – 356Combined sources3
Beta strandi373 – 377Combined sources5
Beta strandi389 – 394Combined sources6
Beta strandi400 – 404Combined sources5
Beta strandi411 – 415Combined sources5
Beta strandi421 – 424Combined sources4
Beta strandi430 – 433Combined sources4
Beta strandi486 – 492Combined sources7
Beta strandi494 – 500Combined sources7
Beta strandi502 – 508Combined sources7
Beta strandi510 – 516Combined sources7
Beta strandi518 – 524Combined sources7
Beta strandi526 – 532Combined sources7
Beta strandi534 – 540Combined sources7
Beta strandi542 – 563Combined sources22
Beta strandi565 – 568Combined sources4
Beta strandi570 – 574Combined sources5

3D structure databases

DisProtiDP00284
ProteinModelPortaliP16009
SMRiP16009
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16009

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 24 family.Curated

Phylogenomic databases

OrthoDBiVOG0900001V

Family and domain databases

InterProiView protein in InterPro
IPR002196 Glyco_hydro_24
IPR010609 Gp5_C
IPR009590 Gp5_OB_N
IPR023346 Lysozyme-like_dom_sf
IPR001165 T4-type_lysozyme
PfamiView protein in Pfam
PF06715 Gp5_C, 3 hits
PF06714 Gp5_OB, 1 hit
PF00959 Phage_lysozyme, 1 hit
PRINTSiPR00684 T4LYSOZYME
SUPFAMiSSF53955 SSF53955, 1 hit

Sequencei

Sequence statusi: Complete.

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

P16009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMISNNLNW FVGVVEDRMD PLKLGRVRVR VVGLHPPQRA QGDVMGIPTE
60 70 80 90 100
KLPWMSVIQP ITSAAMSGIG GSVTGPVEGT RVYGHFLDKW KTNGIVLGTY
110 120 130 140 150
GGIVREKPNR LEGFSDPTGQ YPRRLGNDTN VLNQGGEVGY DSSSNVIQDS
160 170 180 190 200
NLDTAINPDD RPLSEIPTDD NPNMSMAEML RRDEGLRLKV YWDTEGYPTI
210 220 230 240 250
GIGHLIMKQP VRDMAQINKV LSKQVGREIT GNPGSITMEE ATTLFERDLA
260 270 280 290 300
DMQRDIKSHS KVGPVWQAVN RSRQMALENM AFQMGVGGVA KFNTMLTAML
310 320 330 340 350
AGDWEKAYKA GRDSLWYQQT KGRASRVTMI ILTGNLESYG VEVKTPARSL
360 370 380 390 400
SAMAATVAKS SDPADPPIPN DSRILFKEPV SSYKGEYPYV HTMETESGHI
410 420 430 440 450
QEFDDTPGQE RYRLVHPTGT YEEVSPSGRR TRKTVDNLYD ITNADGNFLV
460 470 480 490 500
AGDKKTNVGG SEIYYNMDNR LHQIDGSNTI FVRGDETKTV EGNGTILVKG
510 520 530 540 550
NVTIIVEGNA DITVKGDATT LVEGNQTNTV NGNLSWKVAG TVDWDVGGDW
560 570
TEKMASMSSI SSGQYTIDGS RIDIG
Length:575
Mass (Da):63,116
Last modified:August 1, 1990 - v2
Checksum:i6CC2D04E05155CF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15728 Genomic DNA Translation: CAA33749.1
AF158101 Genomic DNA Translation: AAD42482.1
X14845 Genomic DNA No translation available.
PIRiS25240 G5BPT4
RefSeqiNP_049757.1, NC_000866.4

Genome annotation databases

GeneIDi1258817
KEGGivg:1258817

Similar proteinsi

Entry informationi

Entry nameiBP5_BPT4
AccessioniPrimary (citable) accession number: P16009
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1990
Last modified: May 23, 2018
This is version 129 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, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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