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BPPGK:Q6Y7T6

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Species (Taxon ID) Staphylococcus phage K. (221915)
Gene Name(s) No Information Provided.
Protein Name(s) ORF30/ORF32 (ECO:0000313 with EMBL:AAO47477.2)

Putative endolysin (ECO:0000313 with EMBL:AHB79986.1)

External Links
UniProt Q6Y7T6
EMBL AY176327
KF766114
RefSeq YP_009041293.1
PDB 4CSH
4CT3
PDBsum 4CSH
4CT3
GeneID 19622106
Proteomes UP000001246
GO GO:0046872
GO:0008745
GO:0051715
GO:0009253
Gene3D 3.40.80.10
InterPro IPR002502
IPR007921
IPR003646
Pfam PF01510
PF05257
PF08460
SMART SM00644
SM00287
SUPFAM SSF55846
PROSITE PS50911

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008745

N-acetylmuramoyl-L-alanine amidase activity

PMID:19493008[1]

ECO:0000314

F

Figure 1 shows the EIMS analysis of products of LysK reacting with S.aureus PG. Frame B of figure 1 shows where the enzyme must cut to form the product shown in frame A, between the NAM and the L-ala.

complete
CACAO 6015

GO:0001897

cytolysis by symbiont of host cells

PMID:19493008[1]

ECO:0000314

P

Figure 5 shows LysK is able to lyse various Staph species.

complete
CACAO 6016

GO:0001897

cytolysis by symbiont of host cells

PMID:16199588[2]

ECO:0000314

P

Figure 1 lane 5 shows that extract from E.coli that are induced to express LysK creates a zone of clearing in a zymogram loaded with MRSA cells, indicating lysis.

complete
CACAO 6017

GO:0008233

peptidase activity

PMID:19493008[1]

ECO:0000315

F

Figure 3: A series of LysK deletion constructs were tested using turbidity reduction assays. Constructs lacking the SH3B domain, LysK 211 and 390 showed 10-fold less activity then wild-type LysK. SH3B domains alone, 325-495 showed no discernable activity. 10μL spots containing 10μg of LysK297, or LysK149-495 had no discernable activity in the plate lysis assay. Fusion of SH3B to the CHAP domain, LysK221-390 showed increased activity of the CHAP domain.

complete
CACAO 13103

involved_in

GO:0001897

cytolysis by symbiont of host cells

PMID:19493008[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0001897

cytolysis by symbiont of host cells

PMID:16199588[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008745

N-acetylmuramoyl-L-alanine amidase activity

PMID:19493008[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008745

N-acetylmuramoyl-L-alanine amidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002502
InterPro:IPR036505

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:IPR002502
InterPro:IPR036505

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 Becker, SC et al. (2009) LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells. FEMS Microbiol. Lett. 294 52-60 PubMed GONUTS page
  2. 2.0 2.1 O'Flaherty, S et al. (2005) The recombinant phage lysin LysK has a broad spectrum of lytic activity against clinically relevant staphylococci, including methicillin-resistant Staphylococcus aureus. J. Bacteriol. 187 7161-4 PubMed GONUTS page