ID ENLYS_BPHC1 Reviewed; 186 AA. AC P51728; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 08-NOV-2023, entry version 98. DE RecName: Full=SAR-endolysin {ECO:0000255|HAMAP-Rule:MF_04136}; DE EC=3.2.1.17 {ECO:0000255|HAMAP-Rule:MF_04136}; DE AltName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04136}; DE AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04136}; DE AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04136}; DE AltName: Full=Muramidase {ECO:0000255|HAMAP-Rule:MF_04136}; GN Name=lys; OS Haemophilus phage HP1 (strain HP1c1) (Bacteriophage HP1). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Peduoviridae; Hpunavirus; Haemophilus phage HP1. OX NCBI_TaxID=1289570; OH NCBI_TaxID=727; Haemophilus influenzae. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6098523; DOI=10.1016/0378-1119(84)90208-7; RA Benjamin R.C., Fitzmaurice W.P., Huang P.C., Scocca J.J.; RT "Nucleotide sequence of cloned DNA segments of the Haemophilus influenzae RT bacteriophage HP1c1."; RL Gene 31:173-185(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=8710508; DOI=10.1093/nar/24.12.2360; RA Esposito D., Fitzmaurice W.P., Benjamin R.C., Goodman S.D., Waldman A.S., RA Scocca J.J.; RT "The complete nucleotide sequence of bacteriophage HP1 DNA."; RL Nucleic Acids Res. 24:2360-2368(1996). 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. CC {ECO:0000255|HAMAP-Rule:MF_04136}. 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_04136}; CC -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_04136}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04136}; Periplasmic side {ECO:0000255|HAMAP- CC Rule:MF_04136}. Note=Secreted as a signal-anchored, membrane-tethered, CC inactive endolysin which is subsequently refolded, activated and CC released by membrane depolarization driven by the pinholin. CC {ECO:0000255|HAMAP-Rule:MF_04136}. 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. {ECO:0000255|HAMAP-Rule:MF_04136}. CC -!- PTM: All the periplasmic cyteines of the inactive, membrane-associated CC endolysin are involved in disulfide bond (By similarity). In the active CC soluble form, disulfide bonds are isomerized and only the catalytic CC cysteine remains free (By similarity). {ECO:0000250|UniProtKB:Q37875}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family. CC {ECO:0000255|HAMAP-Rule:MF_04136}. 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; U24159; AAB09211.1; -; Genomic_DNA. DR PIR; S69532; S69532. DR RefSeq; NP_043495.1; NC_001697.1. DR SMR; P51728; -. DR GeneID; 1261120; -. DR KEGG; vg:1261120; -. DR Proteomes; UP000001713; Segment. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR CDD; cd16901; lyz_P1; 1. DR Gene3D; 1.10.530.40; -; 1. DR HAMAP; MF_04110; ENDOLYSIN_T4; 1. DR HAMAP; MF_04136; SAR_ENDOLYSIN; 1. 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 InterPro; IPR043688; SAR_endolysin-like. DR PANTHER; PTHR38107; -; 1. DR PANTHER; PTHR38107:SF4; LYSOZYME; 1. DR Pfam; PF00959; Phage_lysozyme; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. PE 3: Inferred from homology; KW Antimicrobial; Bacteriolytic enzyme; Cytolysis; Disulfide bond; KW Glycosidase; Host cell inner membrane; Host cell lysis by virus; KW Host cell membrane; Host membrane; Hydrolase; Membrane; Reference proteome; KW Signal-anchor; Transmembrane; Transmembrane helix; KW Viral release from host cell. FT CHAIN 1..186 FT /note="SAR-endolysin" FT /id="PRO_0000018519" FT TRANSMEM 1..18 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT ACT_SITE 47 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136" FT ACT_SITE 56 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136" FT DISULFID 11..49 FT /note="In the active soluble endolysin" FT /evidence="ECO:0000250|UniProtKB:Q37875" FT DISULFID 49..56 FT /note="In the inactive membrane-associated endolysin" FT /evidence="ECO:0000250|UniProtKB:Q37875" SQ SEQUENCE 186 AA; 20553 MW; 0203E9A32EF45907 CRC64; MSKKFGAMIL CSAAAVAAAF FAQQKGLPTQ QQNQVSPKAV SMIVNLEGCV RNPYKCPADV WTNGVGNTHN VDKTKILTID EVATDLRRNI KEAENCINTY FNGEKMNQGQ YDAMVSLAFN VGCGNIKTYY SKTQGKRVAT TIYRAAQAEN WILMCNRIED FNKSGGRVLK GLQNRRAKEK ALCLGE //