Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidoglycan hydrolase gp5

Gene

5

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

Functioni

Tail-associated lysozyme of the baseplate hub that is 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. 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.

pH dependencei

Optimum pH is 5.8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei184 – 1841Proton donorBy similarity
Active sitei193 – 1931NucleophileBy similarity
Sitei351 – 3522Cleavage

GO - Molecular functioni

  1. lysozyme activity Source: CACAO
  2. peptidoglycan beta-N-acetylmuramidase activity Source: CACAO

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, Viral tail assembly, Virus entry into host cell, Virus exit from 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:
Peptidoglycan hydrolase gp5 (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 Componenti: Genome

Subcellular locationi

  1. Virion 2 Publications

  2. Note: Present in 3 copies in the baseplate.1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Viral baseplate protein, Viral tail protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Peptidoglycan hydrolase gp5PRO_0000218111Add
BLAST
Chaini1 – 351351Gp5*1 PublicationPRO_0000408360Add
BLAST
Chaini352 – 575224Gp5C1 PublicationPRO_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 (PubMed:12837775, PubMed:19896486, PubMed:11823865). Interacts with gp27 trimer; this interaction forms the tail lysozyme complex (PubMed:12837775). The T4 tail lysozyme complex is made up of three copies of the gp27-gp5*-gp5C complex. Part of the baseplate macromolecular complex which consists of gp5, gp26, gp27, gp28, gp29 (hub); gp6, gp7, gp8, gp10, gp11, gp25, gp53 (wedge); gp9, gp12, gp48 and gp54.1 Publication3 Publications

Binary interactionsi

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

Protein-protein interaction databases

IntActiP16009. 1 interaction.
MINTiMINT-231912.

Structurei

Secondary structure

1
575
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 179Combined sources
Beta strandi27 – 315Combined sources
Turni32 – 343Combined sources
Beta strandi43 – 453Combined sources
Helixi49 – 513Combined sources
Beta strandi54 – 574Combined sources
Beta strandi69 – 713Combined sources
Beta strandi81 – 866Combined sources
Beta strandi94 – 996Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi124 – 1296Combined sources
Helixi131 – 1344Combined sources
Helixi136 – 1405Combined sources
Helixi143 – 1497Combined sources
Beta strandi154 – 1563Combined sources
Turni163 – 1653Combined sources
Helixi176 – 1849Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi204 – 2063Combined sources
Helixi214 – 22512Combined sources
Turni231 – 2344Combined sources
Helixi238 – 25720Combined sources
Helixi262 – 2687Combined sources
Helixi271 – 28414Combined sources
Helixi286 – 2905Combined sources
Helixi293 – 3008Combined sources
Helixi304 – 3118Combined sources
Helixi315 – 3184Combined sources
Turni319 – 3224Combined sources
Helixi323 – 33311Combined sources
Beta strandi334 – 3363Combined sources
Helixi337 – 3393Combined sources
Beta strandi347 – 3504Combined sources
Turni354 – 3563Combined sources
Beta strandi373 – 3775Combined sources
Beta strandi389 – 3946Combined sources
Beta strandi400 – 4045Combined sources
Beta strandi411 – 4155Combined sources
Beta strandi421 – 4244Combined sources
Beta strandi430 – 4334Combined sources
Beta strandi486 – 4927Combined sources
Beta strandi494 – 5007Combined sources
Beta strandi502 – 5087Combined sources
Beta strandi510 – 5167Combined sources
Beta strandi518 – 5247Combined sources
Beta strandi526 – 5327Combined sources
Beta strandi534 – 5407Combined sources
Beta strandi542 – 56322Combined sources
Beta strandi565 – 5684Combined sources
Beta strandi570 – 5745Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4OSDX-ray1.96A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R484-575[»]
DisProtiDP00284.
ProteinModelPortaliP16009.
SMRiP16009. Positions 6-575.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16009.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 24 family.Curated

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

        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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4OSDX-ray1.96A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R484-575[»]
DisProtiDP00284.
ProteinModelPortaliP16009.
SMRiP16009. Positions 6-575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16009. 1 interaction.
MINTiMINT-231912.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258817.
KEGGivg:1258817.

Miscellaneous databases

EvolutionaryTraceiP16009.

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.
ProtoNetiSearch...

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, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "Structure of the bacteriophage T4 baseplate as determined by chemical cross-linking."
    Watts N.R., Coombs D.H.
    J. Virol. 64:143-154(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "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, SUBCELLULAR LOCATION, INTERACTION WITH GP27, SUBUNIT, PROTEOLYTIC CLEAVAGE.
  8. Cited for: REVIEW.
  9. Cited for: REVIEW ON FUNCTION.
  10. "The baseplate wedges of bacteriophage T4 spontaneously assemble into hubless baseplate-like structure in vitro."
    Yap M.L., Mio K., Leiman P.G., Kanamaru S., Arisaka F.
    J. Mol. Biol. 395:349-360(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS).
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
  13. "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 nameiNEEDL_BPT4
AccessioniPrimary (citable) accession number: P16009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1990
Last modified: April 29, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.