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P16009

- VG05_BPT4

UniProt

P16009 - VG05_BPT4

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Protein
Tail-associated lysozyme
Gene
5
Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei184 – 1841Proton donor By similarity
Active sitei193 – 1931Nucleophile By similarity
Sitei351 – 3522Cleavage

GO - Molecular functioni

  1. lysozyme activity Source: CACAO
  2. peptidoglycan beta-N-acetylmuramidase activity Source: CACAO
  3. protein binding Source: IntAct

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
  4. peptidoglycan catabolic process Source: InterPro
  5. viral entry into host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Keywords - Biological processi

Degradation 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, 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:
Tail-associated lysozyme (EC:3.2.1.17)
Alternative name(s):
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 stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000009087: Genome

Subcellular locationi

Virion Inferred

GO - Cellular componenti

  1. virion Source: CACAO
  2. virus tail, baseplate Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Tail-associated lysozyme
PRO_0000218111Add
BLAST
Chaini1 – 351351Gp5*
PRO_0000408360Add
BLAST
Chaini352 – 575224Gp5C
PRO_0000408361Add
BLAST

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

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

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 gp27.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

IntActiP16009. 1 interaction.
MINTiMINT-231912.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 179
Beta strandi27 – 315
Turni32 – 343
Beta strandi43 – 453
Helixi49 – 513
Beta strandi54 – 574
Beta strandi69 – 713
Beta strandi81 – 866
Beta strandi94 – 996
Beta strandi103 – 1064
Beta strandi112 – 1154
Beta strandi117 – 1193
Beta strandi124 – 1296
Helixi131 – 1344
Helixi136 – 1405
Helixi143 – 1497
Beta strandi154 – 1563
Turni163 – 1653
Helixi176 – 1849
Beta strandi187 – 1926
Beta strandi194 – 1963
Beta strandi198 – 2014
Beta strandi204 – 2063
Helixi214 – 22512
Turni231 – 2344
Helixi238 – 25720
Helixi262 – 2687
Helixi271 – 28414
Helixi286 – 2905
Helixi293 – 3008
Helixi304 – 3118
Helixi315 – 3184
Turni319 – 3224
Helixi323 – 33311
Beta strandi334 – 3363
Helixi337 – 3393
Beta strandi347 – 3504
Turni354 – 3563
Beta strandi373 – 3775
Beta strandi389 – 3946
Beta strandi400 – 4045
Beta strandi411 – 4155
Beta strandi421 – 4244
Beta strandi430 – 4334
Beta strandi486 – 4927
Beta strandi494 – 5007
Beta strandi502 – 5087
Beta strandi510 – 5167
Beta strandi518 – 5247
Beta strandi526 – 5327
Beta strandi534 – 5407
Beta strandi542 – 56322
Beta strandi565 – 5684
Beta strandi570 – 5745

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00284.
ProteinModelPortaliP16009.
SMRiP16009. Positions 6-575.

Miscellaneous databases

EvolutionaryTraceiP16009.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.530.40. 1 hit.
InterProiIPR002196. 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]
PfamiPF06715. Gp5_C. 3 hits.
PF06714. Gp5_OB. 1 hit.
PF00959. Phage_lysozyme. 1 hit.
[Graphical view]
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

MEMISNNLNW FVGVVEDRMD PLKLGRVRVR VVGLHPPQRA QGDVMGIPTE    50
KLPWMSVIQP ITSAAMSGIG GSVTGPVEGT RVYGHFLDKW KTNGIVLGTY 100
GGIVREKPNR LEGFSDPTGQ YPRRLGNDTN VLNQGGEVGY DSSSNVIQDS 150
NLDTAINPDD RPLSEIPTDD NPNMSMAEML RRDEGLRLKV YWDTEGYPTI 200
GIGHLIMKQP VRDMAQINKV LSKQVGREIT GNPGSITMEE ATTLFERDLA 250
DMQRDIKSHS KVGPVWQAVN RSRQMALENM AFQMGVGGVA KFNTMLTAML 300
AGDWEKAYKA GRDSLWYQQT KGRASRVTMI ILTGNLESYG VEVKTPARSL 350
SAMAATVAKS SDPADPPIPN DSRILFKEPV SSYKGEYPYV HTMETESGHI 400
QEFDDTPGQE RYRLVHPTGT YEEVSPSGRR TRKTVDNLYD ITNADGNFLV 450
AGDKKTNVGG SEIYYNMDNR LHQIDGSNTI FVRGDETKTV EGNGTILVKG 500
NVTIIVEGNA DITVKGDATT LVEGNQTNTV NGNLSWKVAG TVDWDVGGDW 550
TEKMASMSSI SSGQYTIDGS RIDIG 575
Length:575
Mass (Da):63,116
Last modified:August 1, 1990 - v2
Checksum:i6CC2D04E05155CF5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15728 Genomic DNA. Translation: CAA33749.1 .
AF158101 Genomic DNA. Translation: AAD42482.1 .
X14845 Genomic DNA. No translation available.
PIRi S25240. G5BPT4.
RefSeqi NP_049757.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K28 X-ray 2.90 A 1-575 [» ]
1PDL electron microscopy 12.00 A/B/C 1-575 [» ]
1WTH X-ray 2.80 A 1-575 [» ]
2Z6B X-ray 3.11 A 1-575 [» ]
3A1M X-ray 2.00 A/B/C/D/E/F 490-575 [» ]
4JIV X-ray 1.90 A/B/C 484-575 [» ]
4JIW X-ray 3.40 A/B/C/E/F/G/I/J/K/M/N/O 484-575 [» ]
4JJ2 X-ray 1.28 A/B/C 483-575 [» ]
4KU0 X-ray 1.15 A/B/C 484-575 [» ]
DisProti DP00284.
ProteinModelPortali P16009.
SMRi P16009. Positions 6-575.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P16009. 1 interaction.
MINTi MINT-231912.

Protein family/group databases

CAZyi GH24. Glycoside Hydrolase Family 24.
TCDBi 1.K.1.1.1. the gp27/5 t4-baseplate (t4-bp) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1258817.

Miscellaneous databases

EvolutionaryTracei P16009.

Family and domain databases

Gene3Di 1.10.530.40. 1 hit.
InterProi IPR002196. 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 ]
Pfami PF06715. Gp5_C. 3 hits.
PF06714. Gp5_OB. 1 hit.
PF00959. Phage_lysozyme. 1 hit.
[Graphical view ]
PRINTSi PR00684. T4LYSOZYME.
SUPFAMi SSF53955. SSF53955. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS).
  8. 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).

Entry informationi

Entry nameiVG05_BPT4
AccessioniPrimary (citable) accession number: P16009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1990
Last modified: September 3, 2014
This is version 107 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

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