ENLYS_BPAPS
ID ENLYS_BPAPS Reviewed; 146 AA.
AC Q9T1T5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04110};
DE EC=3.2.1.17 {ECO:0000255|HAMAP-Rule:MF_04110};
DE AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04110};
DE AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04110};
DE AltName: Full=Muramidase {ECO:0000255|HAMAP-Rule:MF_04110};
DE AltName: Full=P13;
GN Name=13;
OS Acyrthosiphon pisum secondary endosymbiont phage 1 (Bacteriophage APSE-1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Sendosyvirus.
OX NCBI_TaxID=2682836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10489345; DOI=10.1006/viro.1999.9902;
RA van der Wilk F., Dullemans A.M., Verbeek M., van den Heuvel J.F.J.M.;
RT "Isolation and characterization of APSE-1, a bacteriophage infecting the
RT secondary endosymbiont of acyrthosiphon pisum.";
RL Virology 262:104-113(1999).
CC -!- FUNCTION: Endolysin with lysozyme activity that degrades host
CC peptidoglycans and participates with the holin and spanin proteins in
CC the sequential events which lead to the programmed host cell lysis
CC releasing the mature viral particles. Once the holin has permeabilized
CC the host cell membrane, the endolysin can reach the periplasm and break
CC down the peptidoglycan layer. {ECO:0000255|HAMAP-Rule:MF_04110}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_04110};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04110}.
CC Note=The endolysin is cytoplasmic, but can reach the periplasmic space
CC with the help of the holins which disrupt the host cell membrane.
CC {ECO:0000255|HAMAP-Rule:MF_04110}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000255|HAMAP-Rule:MF_04110}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF157835; AAF03956.1; -; Genomic_DNA.
DR RefSeq; NP_050974.1; NC_000935.1.
DR SMR; Q9T1T5; -.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR GeneID; 1262307; -.
DR KEGG; vg:1262307; -.
DR Proteomes; UP000000853; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IEA:UniProtKB-UniRule.
DR CDD; cd00737; lyz_endolysin_autolysin; 1.
DR Gene3D; 1.10.530.40; -; 1.
DR HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR InterPro; IPR033907; Endolysin_autolysin.
DR InterPro; IPR034690; Endolysin_T4_type.
DR InterPro; IPR002196; Glyco_hydro_24.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023347; Lysozyme_dom_sf.
DR Pfam; PF00959; Phage_lysozyme; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 3: Inferred from homology;
KW Antimicrobial; Bacteriolytic enzyme; Cytolysis; Glycosidase;
KW Host cell lysis by virus; Host cytoplasm; Hydrolase; Reference proteome;
KW Viral release from host cell.
FT CHAIN 1..146
FT /note="Endolysin"
FT /id="PRO_0000218091"
FT ACT_SITE 15
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04110"
FT ACT_SITE 24
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04110"
SQ SEQUENCE 146 AA; 16330 MW; AF9689BC02218086 CRC64;
MHISEKGLVL IKRYEGLRLK AYQCRAGRWT LGYGHTHNLN IGDVITQEQA EAFLREDIAQ
VTALLNTQIK VPLTQNQYDA ICSLVFNIGM TAFTTSTLLK KLNVGDYSGA SAEFMKWSKA
KVNGKRTPLP GLIKRRQAEK ALFESA
