BPT4:BP5

Species (Taxon ID)	Enterobacteria phage T4 (Bacteriophage T4). (10665)
Gene Name(s)	5
Protein Name(s)	Baseplate central spike complex protein gp5 (ECO:0000303 with PMID:27193680^[1]) Peptidoglycan hydrolase gp5 Protein Gp5 Gp5* Gp5C
External Links
UniProt	P16009
EMBL	X15728 AF158101 X14845
PIR	S25240
RefSeq	NP_049757.1
PDB	1K28 1PDL 1WTH 2Z6B 3A1M 4JIV 4JIW 4JJ2 4KU0 4OSD 5IV5
PDBsum	1K28 1PDL 1WTH 2Z6B 3A1M 4JIV 4JIW 4JJ2 4KU0 4OSD 5IV5
DisProt	DP00284
ProteinModelPortal	P16009
SMR	P16009
IntAct	P16009
MINT	MINT-231912
CAZy	GH24
TCDB	1.K.1.1.1
GeneID	1258817
KEGG	vg:1258817
OrthoDB	VOG0900001V
EvolutionaryTrace	P16009
Proteomes	UP000009087
GO	GO:0019012 GO:0098025 GO:0003796 GO:0033922 GO:0016998 GO:0019835 GO:0042742 GO:0085027 GO:0009253 GO:0046718 GO:0019076
Gene3D	1.10.530.40
InterPro	IPR002196 IPR010609 IPR009590 IPR023346 IPR023347 IPR001165
Pfam	PF06715 PF06714 PF00959
PRINTS	PR00684
SUPFAM	SSF53955

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0003796	lysozyme activity	PMID:3157805^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0098025	virus tail, baseplate	PMID:27193680^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003796	lysozyme activity	PMID:15701513^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0098015	virus tail	PMID:15701513^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0009405	pathogenesis	PMID:15701513^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15701513^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0070207	protein homotrimerization	PMID:15701513^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0085027	entry into host via enzymatic degradation of host anatomical structure	PMID:3157805^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0098025	virus tail, baseplate	PMID:3157805^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0098025	virus tail, baseplate	PMID:10217762^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0033922	peptidoglycan beta-N-acetylmuramidase activity	PMID:3157805^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0019012	virion	PMID:18524932^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003796	lysozyme activity	PMID:10217762^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003796	lysozyme activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001165 InterPro:IPR002196	F	Seeded From UniProt	complete
involved_in	GO:0009253	peptidoglycan catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002196	P	Seeded From UniProt	complete
involved_in	GO:0016998	cell wall macromolecule catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001165 InterPro:IPR002196	P	Seeded From UniProt	complete
enables	GO:0003796	lysozyme activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.17	F	Seeded From UniProt	complete
involved_in	GO:0098932	disruption by virus of host cell wall peptidoglycan during virus entry	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1236	P	Seeded From UniProt	complete
involved_in	GO:0098994	disruption of host cell envelope during viral entry	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1235	P	Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1162 UniProtKB-KW:KW-1160	P	Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	F	Seeded From UniProt	complete
part_of	GO:0098025	virus tail, baseplate	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1226	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0019835	cytolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0081	P	Seeded From UniProt	complete
part_of	GO:0019012	virion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0946 UniProtKB-SubCell:SL-0274	C	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0081	F	Seeded From UniProt	complete
involved_in	GO:0042742	defense response to bacterium	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0081	P	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0081 UniProtKB-KW:KW-0326	P	Seeded From UniProt	complete
involved_in	GO:0098003	viral tail assembly	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1245	P	Seeded From UniProt	complete
part_of	GO:0098015	virus tail	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1227	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Taylor, NM et al. (2016) Structure of the T4 baseplate and its function in triggering sheath contraction. Nature 533 346-52 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Nakagawa, H et al. (1985) Isolation and characterization of the bacteriophage T4 tail-associated lysozyme. J. Virol. 54 460-6 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Kanamaru, S et al. (2005) Control of bacteriophage T4 tail lysozyme activity during the infection process. J. Mol. Biol. 346 1013-20 PubMed GONUTS page
↑ ^4.0 ^4.1 Kanamaru, S et al. (1999) The C-terminal fragment of the precursor tail lysozyme of bacteriophage T4 stays as a structural component of the baseplate after cleavage. J. Bacteriol. 181 2739-44 PubMed GONUTS page
↑ Clokie, MR et al. (2008) A proteomic approach to the identification of the major virion structural proteins of the marine cyanomyovirus S-PM2. Microbiology (Reading, Engl.) 154 1775-82 PubMed GONUTS page

[PMID:27193680-1] 1.0 ^1.1 Taylor, NM et al. (2016) Structure of the T4 baseplate and its function in triggering sheath contraction. Nature 533 346-52 PubMed GONUTS page

[PMID:3157805-2] 2.0 ^2.1 ^2.2 ^2.3 Nakagawa, H et al. (1985) Isolation and characterization of the bacteriophage T4 tail-associated lysozyme. J. Virol. 54 460-6 PubMed GONUTS page

[PMID:15701513-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Kanamaru, S et al. (2005) Control of bacteriophage T4 tail lysozyme activity during the infection process. J. Mol. Biol. 346 1013-20 PubMed GONUTS page

[PMID:10217762-4] 4.0 ^4.1 Kanamaru, S et al. (1999) The C-terminal fragment of the precursor tail lysozyme of bacteriophage T4 stays as a structural component of the baseplate after cleavage. J. Bacteriol. 181 2739-44 PubMed GONUTS page

[PMID:18524932-5] Clokie, MR et al. (2008) A proteomic approach to the identification of the major virion structural proteins of the marine cyanomyovirus S-PM2. Microbiology (Reading, Engl.) 154 1775-82 PubMed GONUTS page

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BPT4:BP5

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