AC   MF_04136;
DC   Protein; auto
TR   HAMAP; MF_04136; -; 1; level=0
XX
Names: SAR_ENDOLYSIN
XX
ID   ENLYS
DE   RecName: Full=SAR-endolysin;
DE            EC=3.2.1.17;
DE   AltName: Full=Endolysin;
DE   AltName: Full=Lysis protein;
DE   AltName: Full=Lysozyme;
DE   AltName: Full=Muramidase;
XX
case <OC:Muvirus>
CC   -!- FUNCTION: Signal-arrest-release (SAR) endolysin with lysozyme activity
CC       that degrades host peptidoglycans and participates with the releasin
CC       and spanin proteins in the sequential events which lead to programmed
CC       host cell lysis releasing the mature viral particles. The SAR-endolysin
CC       is released by the releasin protein into the periplasm, where it breaks
CC       down the peptidoglycan layer.
else
CC   -!- FUNCTION: Signal-arrest-release (SAR) endolysin with lysozyme activity
CC       that degrades host peptidoglycans and participates with the pinholin
CC       and spanin proteins in the sequential events which lead to programmed
CC       host cell lysis releasing the mature viral particles. Once the pinholin
CC       has permeabilized the host cell membrane, the SAR-endolysin is released
CC       into the periplasm where it breaks down the peptidoglycan layer.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17;
case <AnyFeature:Transmembrane<2>
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane; Single-pass type II
CC       membrane protein; Periplasmic side. Note=Secreted as a signal-anchored,
CC       membrane-tethered, inactive endolysin which is subsequently refolded,
CC       activated and released by membrane depolarization driven by the
CC       pinholin.
CC   -!- DOMAIN: The signal-anchor, which may also be an uncleaved signal
CC       sequence tethers the SAR-endolysin to the membrane until the latter is
CC       depolarized by the holin, resulting in the escape of SAR-endolysin from
CC       the membrane.
end case
case <FTGroup:1>
CC   -!- PTM: All the periplasmic cyteines of the inactive, membrane-associated
CC       endolysin are involved in disulfide bond. In the active soluble form,
CC       disulfide bonds are isomerized and only the catalytic cysteine remains
CC       free.
end case
case not <FTTag:Act_site> and not <FTTag:Act_site_Cys>
CC   -!- CAUTION: Lacks the conserved Asp active site.
end case
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
XX
DR   Pfam; PF00959; Phage_lysozyme; 1; trigger=no
case <AnyFeature:Transmembrane<2>
DR   General; Transmembrane; -; 1; trigger=yes
end case
XX
KW   Antimicrobial
KW   Bacteriolytic enzyme
KW   Cytolysis
KW   Glycosidase
KW   Host cell inner membrane
KW   Host cell lysis by virus
KW   Host cell membrane
KW   Host membrane
KW   Hydrolase
KW   Membrane
KW   Signal-anchor
KW   Transmembrane
KW   Transmembrane helix
KW   Viral release from host cell
case <FTGroup:1>
KW   Disulfide bond
end case
XX
GO   GO:0003796; F:lysozyme activity
GO   GO:0044659; P:viral release from host cell by cytolysis
GO   GO:0009253; P:peptidoglycan catabolic process
XX
FT   From: ENLYS_BPKMV (Q7Y2C0)
case not <AnyFeature:Transmembrane>
FT   TRANSMEM        1..19
FT                   /note="Helical; Signal-anchor for type II membrane protein"
end case
FT   ACT_SITE        21
FT                   /note="Proton donor/acceptor"
FT   Optional; Condition: E
FT   ACT_SITE        30
FT                   /note="Proton donor/acceptor"
FT   Tag: Act_site; Optional; Condition: D
FT   From: ENLYS_BPP1 (Q37875)
FT   ACT_SITE        51
FT                   /note="Proton donor/acceptor"
FT   Tag: Act_site_Cys; Optional; Condition: C
FT   DISULFID        13..44
FT                   /note="In the active soluble endolysin; alternate"
FT   Group: 1; Condition: C-x*-C
FT   DISULFID        44..51
FT                   /note="In the inactive membrane-associated endolysin;
FT                   alternate"
FT   Group: 1; Condition: C-x*-C
XX
Size: 140-250;
Related: MF_04110;
Template: Q7Y2C0; P27359; Q37875;
Scope:
 Viruses
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.6 2022/08/09
//