BPP22:EXLYS

Species (Taxon ID)	Enterobacteria phage P22 (Bacteriophage P22). (10754)
Gene Name(s)	4
Protein Name(s)	Peptidoglycan hydrolase gp4 Gene product 4 Gp4 Internal virion protein gp4
External Links
UniProt	P26746
EMBL	M59749 AF217253 BK000583
PIR	F40474
RefSeq	NP_059632.1
PDB	4V4K 5GAI
PDBsum	4V4K 5GAI
DIP	DIP-59582N
GeneID	1262828
KEGG	vg:1262828
Proteomes	UP000001795 UP000007960
GO	GO:0019012 GO:0016787 GO:0046718
InterPro	IPR020362
Pfam	PF11650
ProDom	PD097046

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0098015	virus tail	PMID:16970964	ECO:0000314			C		Figure 9. Negative stain electron microscopy of tail accessory factor gp4 bound to P22 portal protein rings. (a) Negative stain electron microscopy image of purified P22 portal protein rings. Many “donut-like” structures are visible, which in most (rarer) side view cases adopt a head-to-head conformation. (b) Negative stain micrograph of gel filtration purified portal protein in complex with gp4. Micrographs of the gp1:gp4 complex were compared to gp4-free portal rings, as shown in Figure 9(a) and (b), respectively. The majority of gp1:gp4 complexes seen on the micrographs displayed a preferential orientation on the grid with the central hole perpendicular to the grid. In rare instances single complexes and head-tohead dimers of the gp1:gp4 complex were seen in side view (see higher magnifications in Figure 9(b))	complete CACAO 12028
	GO:0046798	viral portal complex	PMID:16970964	ECO:0000314			C		Figure 7. Isolating the gp1:gp4 assembly intermediate on agarose gel. (a) Native agarose gel run at 30 °C showing a stably populated gp(1)12:gp(4)6 assembly intermediate. In lane 1 is dodecameric portal protein gp(1)12. The gp(1)12:gp(4)6 assembly intermediate in lanes 2 and 3 migrates on gel as a slightly lower mobility band, clearly distinguishable from fully saturated decorated gp(1)12:gp(4)12 complex in lane 4 and free dodecameric portal protein gp(1)12 in lane 4. The intermediates in lanes 2 and 3 were formed by adding six equivalents of gp4 to gp(1)12 and incubating the complex at 30 °C for 30 s and 30 min, respectively. In lane 4 approximately eight equivalents of gp4 were added, yielding the fully decorated gp(1)12:gp(4)12 complex and free gp(1)12. (b) Titration of gp4 binding to gp1 at 30 °C. By running the agarose gel at 30 °C both gp(1)12:gp(4)6 assembly intermediate and fully decorated gp(1)12:gp(4)12 portal protein are visible on the same titration. The assembly intermediate appears at stoichiometries gp(1):gp(4) equal to 12 (lanes 3−6) and fades away in lane 7, where >six equivalents of gp4 are present. Micrographs of the gp1:gp4 complex were compared to gp4-free portal rings, as shown in Figure 9(a) and (b), respectively. The majority of gp1:gp4 complexes seen on the micrographs displayed a preferential orientation on the grid with the central hole perpendicular to the grid. In rare instances single complexes and head-tohead dimers of the gp1:gp4 complex were seen in side view (see higher magnifications in Figure 9(b)). Such side views are particularly informative, in that the dodecameric portal protein without bound gp4 forms a mushroom-shaped structure with a channel through the center	complete CACAO 12031
	GO:0019073	viral DNA genome packaging	PMID:6363718	ECO:0000315			P		Fro. I. Dependenc~ of phage formation in vitro on the concentration of the capsid donor extract. Infected ¢~zl[ extracts containing incomplete capsids were freshly thawed and lysed as described in Materials and Methods. D~uted .samples were mixed with concentrated protein donor extract {5-) and incubated for I h at 23°C, at which time the reactions were stopped by further dilution and titered for viable phage. The background of the protein donor extract was 102 phage/mi. The background of the • at mo.~l, Conc-entrated calmid donor extracts were (0) 3.3× 10 (4- extract), (t) 2:5 × l0 T (10- extract) and (at) 2 x 103 (26-extract). Fro. 4. Dependence of in vitro a.~.~em!~ly on the concentration of the 4", lO ÷ and 26* activities. (a) Com|)lementation of 10- extracts (O), 26- extracts (11) and 4- extracts (~lk) with protein donor extract. The cap,aid extracts were diluted 25-fold, to a final infected cell cont'entration of about 2 x 10 ° c~lls/ml. Samples were mixed with serial dilutions of the 5- prc)tein donor. The maximum slo|~s determined from these curve,a were: 4+ activity, 5 to 6; 26 + activity. I to 2; 10 + activity, 4 to 5. The background of the undiluted extracts were protein donor 10a; 4- extract < 10s; 10- extracts, 5 x 10~; 26- extract, 2 x l0 a. (b) Variation of the ratio of cap`aid,a to protein; complemcntation of 4- ~'apsids with cap,aid donor cell concentration: (O) 5x lO 9 cell,a/ml; (A) 2 x l0 s cell,a/ml; (m) 4 x i0 v (~lls/ml. The protein donor extract was from the same batch a.s used in (a).	complete CACAO 12032
	GO:0019073	viral DNA genome packaging	PMID:21439834	ECO:0000314			P		Comparing the portal position in the procapsid and the virion shows that the portal increases its contact with the capsid shell during maturation (Figure S1). We propose that this portion of the scaffold remains in place during dsDNA packaging, allowing access of the gp4 C terminus to the bottom of the portal. When gp4 binds, the scaffold protein is displaced allowing the final conformational change implied by the position of the gp4-C-terminal polypeptide that is wedged between the capsid and portal.	complete CACAO 12035
involved_in	GO:0099002	viral genome ejection through host cell envelope, short tail mechanism	PMID:21499245	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0098932	disruption by virus of host cell wall peptidoglycan during virus entry	PMID:14763988	ECO:0000314	direct assay evidence used in manual assertion		P		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
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
involved_in	GO:0099002	viral genome ejection through host cell envelope, short tail mechanism	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1244	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-1160 UniProtKB-KW:KW-1162	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
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
edit table

References

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