Tail-associated lysozyme - Enterobacteria phage T4

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P16009 (VG05_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tail-associated lysozyme
EC=3.2.1.17

Alternative name(s):
Protein Gp5

Gene names

Name:

Organism

Enterobacteria phage T4 (Bacteriophage T4) [Reference proteome]

Taxonomic identifier

10665 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4likevirus ›

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
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.

Ontologies

Keywords
Biological process	Viral genome injection through bacterial membranes Viral penetration into host cytoplasm Virus entry into host cell
Developmental stage	Late protein
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro viral entry into host cell Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	lysozyme activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
27	P17172	2	EBI-1032754,EBI-1032762

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 575

575

Tail-associated lysozyme

PRO_0000218111

Chain

1 – 351

351

Gp5*

PRO_0000408360

Chain

352 – 575

224

Gp5C

PRO_0000408361

Sites

Active site

184

Proton donor By similarity

Active site

193

Nucleophile By similarity

Site

351 – 352

Cleavage

Secondary structure

575

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P16009 [UniParc].

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

FASTA

575

63,116

        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' referencesShow '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.

PIR

G5BPT4. S25240.

RefSeq

NP_049757.1. NC_000866.4.

3D structure databases

PDBe
RCSB PDB
PDBj

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	491-575	[»]

DisProt

DP00284.

ProteinModelPortal

P16009.

SMR

P16009. Positions 6-575.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16009. 1 interaction.

MINT

MINT-231912.

Protein family/group databases

CAZy

GH24. Glycoside Hydrolase Family 24.

TCDB

9.B.11.1.1. Gp27/5 T4-baseplate (T4-BP) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1258817.

Phylogenomic databases

ProtClustDB

PHA2596.

Family and domain databases

Gene3D

1.10.530.40. 1 hit.

InterPro

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]

Pfam

PF06715. Gp5_C. 3 hits.
PF06714. Gp5_OB. 1 hit.
PF00959. Phage_lysozyme. 1 hit.
[Graphical view]

PRINTS

PR00684. T4LYSOZYME.

SUPFAM

SSF53955. SSF53955. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P16009.

Entry information

Entry name

VG05_BPT4

Accession

Primary (citable) accession number: P16009

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents