BPP1:ENLYS

Species (Taxon ID)	Escherichia phage P1 (Bacteriophage P1). (10678)
Gene Name(s)	17 (synonyms: lysa, lyz)
Protein Name(s)	SAR-endolysin (ECO:0000255 with HAMAP-Rule:MF_04136) Endolysin (ECO:0000255 with HAMAP-Rule:MF_04136) Gene product 17 gp17 Lysis protein (ECO:0000255 with HAMAP-Rule:MF_04136) Lysozyme (ECO:0000255 with HAMAP-Rule:MF_04136, ECO:0000303 with PMID:15637279^[1]) Muramidase (ECO:0000255 with HAMAP-Rule:MF_04136)
External Links
UniProt	Q37875
EMBL	X87673 AF125376 AF234172
RefSeq	YP_006484.1
PDB	1XJT 1XJU
PDBsum	1XJT 1XJU
SMR	Q37875
DrugBank	DB04272
CAZy	GH24
PRIDE	Q37875
GeneID	2777454
KEGG	vg:2777454
KO	K01185
EvolutionaryTrace	Q37875
Proteomes	UP000008091
GO	GO:0020002 GO:0016021 GO:0003796 GO:0016998 GO:0019835 GO:0042742 GO:0009253
HAMAP	MF_04110 MF_04136
InterPro	IPR002196 IPR023346
Pfam	PF00959
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	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002196	F	Seeded From UniProt
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
involved_in	GO:0016998	cell wall macromolecule catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002196	P	Seeded From UniProt
enables	GO:0003796	lysozyme activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.17	F	Seeded From UniProt
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1030 UniProtKB-KW:KW-1032 UniProtKB-SubCell:SL-0373	C	Seeded From UniProt
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
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt
involved_in	GO:0019835	cytolysis	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0081 UniProtKB-KW:KW-0204	P	Seeded From UniProt
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
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
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C	Seeded From UniProt
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
part_of	GO:0033644	host cell membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1043	C	Seeded From UniProt
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
enables	GO:0003796	lysozyme activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002196	F	Seeded From UniProt
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
involved_in	GO:0016998	cell wall macromolecule catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002196	P	Seeded From UniProt
enables	GO:0003796	lysozyme activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.17	F	Seeded From UniProt
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1030 UniProtKB-KW:KW-1032 UniProtKB-SubCell:SL-0373	C	Seeded From UniProt
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
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt
involved_in	GO:0019835	cytolysis	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0081 UniProtKB-KW:KW-0204	P	Seeded From UniProt
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
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
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C	Seeded From UniProt
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
involved_in	GO:0019835	cytolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0204	P	Seeded From UniProt
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1032	C	Seeded From UniProt
part_of	GO:0033644	host cell membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1043	C	Seeded From UniProt
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
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	P	Seeded From UniProt
	GO:0033644	host cell membrane	PMID:15090650^[2]	ECO:0006042	cell fractionation evidence used in manual assertion		C	Fig. 3 shows presence of Lyz in membrane fraction. UniProtKB: Q37875 (ENLYS_BPP1) Organism: Escherichia phage P1 (Bacteriophage P1) UniProt submitted name: SAR-endolysin	complete
part_of	GO:0020002	host cell plasma membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0373	C	Seeded From UniProt
	GO:0033646	host intracellular part	PMID:15090650^[2]	ECO:0006042	cell fractionation evidence used in manual assertion		C	Fig. 3 shows presence of Lyz in soluble fraction. UniProtKB: Q37875 (ENLYS_BPP1) Organism: Escherichia phage P1 (Bacteriophage P1) UniProt submitted name: SAR-endolysin	complete
	GO:0042597	periplasmic space	PMID:15090650^[2]	ECO:0006042	cell fractionation evidence used in manual assertion		C	Fig. 3B shows presence of Lyz in periplasmic fractions. UniProtKB: Q37875 (ENLYS_BPP1) Organism: Escherichia phage P1 (Bacteriophage P1) UniProt submitted name: SAR-endolysin	complete
	GO:0019835	cytolysis	PMID:15090650^[2]	ECO:0007699	cell growth assay evidence used in manual assertion		P	Fig. 1A shows culture clearing after induction of recombinant Lys in XL1-Blue cells. UniProtKB: Q37875 (ENLYS_BPP1) Organism: Escherichia phage P1 (Bacteriophage P1) UniProt submitted name: SAR-endolysin	complete
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Notes

References

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

↑ Xu, M et al. (2005) Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science 307 113-7 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Xu, M et al. (2004) A signal-arrest-release sequence mediates export and control of the phage P1 endolysin. Proc. Natl. Acad. Sci. U.S.A. 101 6415-20 PubMed GONUTS page

[PMID:15637279-1] Xu, M et al. (2005) Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science 307 113-7 PubMed GONUTS page

[PMID:15090650-2] 2.0 ^2.1 ^2.2 ^2.3 Xu, M et al. (2004) A signal-arrest-release sequence mediates export and control of the phage P1 endolysin. Proc. Natl. Acad. Sci. U.S.A. 101 6415-20 PubMed GONUTS page

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BPP1:ENLYS

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