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P16009 (VG05_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tail-associated lysozyme

EC=3.2.1.17
Alternative name(s):
Protein Gp5

Cleaved into the following 2 chains:

  1. Gp5*
  2. Gp5C
Gene names
Name:5
OrganismEnterobacteria phage T4 (Bacteriophage T4) [Reference proteome]
Taxonomic identifier10665 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tail-associated lysozyme essential for localized hydrolysis of bacterial cell wall necessary for viral DNA injection. The needle-like gp5 protein punctures the outer cell membrane and then digests the peptidoglycan cell wall in the periplasmic space. Ref.6

Catalytic activity

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.

Subunit structure

Homotrimer. Interacts with gp27; this interaction forms the tail lysozyme complex. The T4 tail lysozyme complex is made up of three copies of the proteolytically processed gp5 and three copies of gp27. Ref.6

Subcellular location

Virion Probable.

Post-translational modification

In the fully assembled virus, gp5 is cleaved after residue 351, but the resulting fragments, gp5* and gp5C, remain associated with the virion. Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 24 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

27P171722EBI-1032754,EBI-1032762

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Tail-associated lysozyme
PRO_0000218111
Chain1 – 351351Gp5*
PRO_0000408360
Chain352 – 575224Gp5C
PRO_0000408361

Sites

Active site1841Proton donor By similarity
Active site1931Nucleophile By similarity
Site351 – 3522Cleavage

Secondary structure

...................................................................................................... 575
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16009 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 6CC2D04E05155CF5

FASTA57563,116
        10         20         30         40         50         60 
MEMISNNLNW FVGVVEDRMD PLKLGRVRVR VVGLHPPQRA QGDVMGIPTE KLPWMSVIQP 

        70         80         90        100        110        120 
ITSAAMSGIG GSVTGPVEGT RVYGHFLDKW KTNGIVLGTY GGIVREKPNR LEGFSDPTGQ 

       130        140        150        160        170        180 
YPRRLGNDTN VLNQGGEVGY DSSSNVIQDS NLDTAINPDD RPLSEIPTDD NPNMSMAEML 

       190        200        210        220        230        240 
RRDEGLRLKV YWDTEGYPTI GIGHLIMKQP VRDMAQINKV LSKQVGREIT GNPGSITMEE 

       250        260        270        280        290        300 
ATTLFERDLA DMQRDIKSHS KVGPVWQAVN RSRQMALENM AFQMGVGGVA KFNTMLTAML 

       310        320        330        340        350        360 
AGDWEKAYKA GRDSLWYQQT KGRASRVTMI ILTGNLESYG VEVKTPARSL SAMAATVAKS 

       370        380        390        400        410        420 
SDPADPPIPN DSRILFKEPV SSYKGEYPYV HTMETESGHI QEFDDTPGQE RYRLVHPTGT 

       430        440        450        460        470        480 
YEEVSPSGRR TRKTVDNLYD ITNADGNFLV AGDKKTNVGG SEIYYNMDNR LHQIDGSNTI 

       490        500        510        520        530        540 
FVRGDETKTV EGNGTILVKG NVTIIVEGNA DITVKGDATT LVEGNQTNTV NGNLSWKVAG 

       550        560        570 
TVDWDVGGDW TEKMASMSSI SSGQYTIDGS RIDIG 

« Hide

References

« Hide 'large scale' references
[1]"Functional relationships and structural determinants of two bacteriophage T4 lysozymes: a soluble (gene e) and a baseplate-associated (gene 5) protein."
Mosig G., Lin G.W., Franklin J., Fan W.H.
New Biol. 1:171-179(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Mosig G.
Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Bacteriophage T4 genome."
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.
Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Sequencing, cloning and overexpression of genes of bacteriophage T4 between map positions 74.325 and 77.184."
Koch T., Lamm N., Rueger W.
Nucleic Acids Res. 17:4392-4392(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
[5]"Isolation and characterization of the bacteriophage T4 tail-associated lysozyme."
Nakagawa H., Arisaka F., Ishii S.
J. Virol. 54:460-466(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, CHARACTERIZATION.
[6]"Homotrimeric, beta-stranded viral adhesins and tail proteins."
Weigele P.R., Scanlon E., King J.
J. Bacteriol. 185:4022-4030(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH GP27, PROTEOLYTIC CLEAVAGE.
[7]"Three-dimensional structure of bacteriophage T4 baseplate."
Kostyuchenko V.A., Leiman P.G., Chipman P.R., Kanamaru S., van Raaij M.J., Arisaka F., Mesyanzhinov V.V., Rossmann M.G.
Nat. Struct. Biol. 10:688-693(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS).
[8]"Structure of the cell-puncturing device of bacteriophage T4."
Kanamaru S., Leiman P.G., Kostyuchenko V.A., Chipman P.R., Mesyanzhinov V.V., Arisaka F., Rossmann M.G.
Nature 415:553-557(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[9]"Control of bacteriophage T4 tail lysozyme activity during the infection process."
Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., Arisaka F.
J. Mol. Biol. 346:1013-1020(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15728 Genomic DNA. Translation: CAA33749.1.
AF158101 Genomic DNA. Translation: AAD42482.1.
X14845 Genomic DNA. No translation available.
PIRG5BPT4. S25240.
RefSeqNP_049757.1. NC_000866.4.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K28X-ray2.90A1-575[»]
1PDLelectron microscopy12.00A/B/C1-575[»]
1WTHX-ray2.80A1-575[»]
2Z6BX-ray3.11A1-575[»]
3A1MX-ray2.00A/B/C/D/E/F490-575[»]
4JIVX-ray1.90A/B/C484-575[»]
4JIWX-ray3.40A/B/C/E/F/G/I/J/K/M/N/O484-575[»]
4JJ2X-ray1.28A/B/C483-575[»]
4KU0X-ray1.15A/B/C484-575[»]
DisProtDP00284.
ProteinModelPortalP16009.
SMRP16009. Positions 6-575.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP16009. 1 interaction.
MINTMINT-231912.

Protein family/group databases

CAZyGH24. Glycoside Hydrolase Family 24.
TCDB1.K.1.1.1. the gp27/5 t4-baseplate (t4-bp) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1258817.

Family and domain databases

Gene3D1.10.530.40. 1 hit.
InterProIPR002196. Glyco_hydro_24.
IPR010609. Gp5_C.
IPR009590. Gp5_OB_N_virus.
IPR023346. Lysozyme-like_dom.
IPR023347. Lysozyme_dom.
IPR001165. Phage_T4_Gp5_lysozyme.
[Graphical view]
PfamPF06715. Gp5_C. 3 hits.
PF06714. Gp5_OB. 1 hit.
PF00959. Phage_lysozyme. 1 hit.
[Graphical view]
PRINTSPR00684. T4LYSOZYME.
SUPFAMSSF53955. SSF53955. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP16009.

Entry information

Entry nameVG05_BPT4
AccessionPrimary (citable) accession number: P16009
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries