ENLYS_BPMU
ID ENLYS_BPMU Reviewed; 171 AA.
AC Q9T1X2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 29-SEP-2021, entry version 87.
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=Gene product 22;
DE Short=gp22;
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; OrderedLocusNames=Mup22;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [2]
RP INDUCTION.
RX PubMed=2524470; DOI=10.1128/jb.171.6.3440-3448.1989;
RA Stoddard S.F., Howe M.M.;
RT "Localization and regulation of bacteriophage Mu promoters.";
RL J. Bacteriol. 171:3440-3448(1989).
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 -!- INDUCTION: Expressed in the intermediate phase of the viral replicative
CC cycle. {ECO:0000269|PubMed:2524470}.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000255|HAMAP-Rule:MF_04136}.
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DR EMBL; AF083977; AAF01099.1; -; Genomic_DNA.
DR RefSeq; NP_050626.1; NC_000929.1.
DR SMR; Q9T1X2; -.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR GeneID; 2636261; -.
DR KEGG; vg:2636261; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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: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:InterPro.
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 Pfam; PF00959; Phage_lysozyme; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 2: Evidence at transcript level;
KW Antimicrobial; Bacteriolytic enzyme; Cytolysis; Glycosidase;
KW Host cell inner membrane; Host cell lysis by virus; Host cell membrane;
KW Host membrane; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Viral release from host cell.
FT CHAIN 1..171
FT /note="SAR-endolysin"
FT /id="PRO_0000218096"
FT TRANSMEM 1..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT ACT_SITE 37
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
FT ACT_SITE 46
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
SQ SEQUENCE 171 AA; 18884 MW; 9F53C6ADF47D4789 CRC64;
MAGIPKKLKA ALLAVTIAGG GVGGYQEMTR QSLIHLENIA YMPYRDIAGV LTVCVGHTGP
DIEMRRYSHA ECMALLDSDL KPVYAAIDRL VRVPLTPYQK TALATFIFNT GVTAFSKSTL
LKKLNAGDYA GARDQMARWV FAAGHKWKGL MNRREVEMAI WNIRGADDLR Q
