ENLYS_BPKMV
ID ENLYS_BPKMV Reviewed; 160 AA.
AC Q7Y2C0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 29-SEP-2021, entry version 88.
DE RecName: Full=SAR-endolysin {ECO:0000255|HAMAP-Rule:MF_04136, ECO:0000303|PubMed:21687532};
DE EC=3.2.1.17 {ECO:0000255|HAMAP-Rule:MF_04136, ECO:0000269|PubMed:21687532};
DE AltName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04136};
DE AltName: Full=Gene product 45;
DE Short=gp45;
DE AltName: Full=KMV45 {ECO:0000303|PubMed:21687532};
DE AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04136, ECO:0000305};
DE AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04136};
DE AltName: Full=Muramidase {ECO:0000255|HAMAP-Rule:MF_04136, ECO:0000303|PubMed:21687532};
GN Name=45;
OS Pseudomonas phage phiKMV.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Krylovirinae; Phikmvvirus.
OX NCBI_TaxID=204270;
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12890620; DOI=10.1016/s0042-6822(03)00123-5;
RA Lavigne R., Burkal'tseva M.V., Robben J., Sykilinda N.N., Kurochkina L.P.,
RA Grymonprez B., Jonckx B., Krylov V.N., Mesyanzhinov V.V., Volckaert G.;
RT "The genome of bacteriophage phiKMV, a T7-like virus infecting Pseudomonas
RT aeruginosa.";
RL Virology 312:49-59(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15549178; DOI=10.1007/s00018-004-4301-y;
RA Lavigne R., Briers Y., Hertveldt K., Robben J., Volckaert G.;
RT "Identification and characterization of a highly thermostable bacteriophage
RT lysozyme.";
RL Cell. Mol. Life Sci. 61:2753-2759(2004).
RN [3]
RP CHARACTERIZATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21687532; DOI=10.4161/bact.1.1.14868;
RA Briers Y., Peeters L.M., Volckaert G., Lavigne R.;
RT "The lysis cassette of bacteriophage varphiKMV encodes a signal-arrest-
RT release endolysin and a pinholin.";
RL Bacteriophage 1:25-30(2011).
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, ECO:0000305|PubMed:21687532}.
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 ECO:0000269|PubMed:21687532};
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, ECO:0000269|PubMed:21687532}.
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 ECO:0000269|PubMed:21687532}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000255|HAMAP-Rule:MF_04136}.
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DR EMBL; AJ505558; CAD44236.1; -; Genomic_DNA.
DR RefSeq; NP_877484.1; NC_005045.1.
DR SMR; Q7Y2C0; -.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR GeneID; 1482618; -.
DR KEGG; vg:1482618; -.
DR Proteomes; UP000000842; 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 1: Evidence at protein 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..160
FT /note="SAR-endolysin"
FT /id="PRO_0000429256"
FT TRANSMEM 1..19
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
FT TOPO_DOM 20..160
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21687532"
FT ACT_SITE 21
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
FT ACT_SITE 30
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
SQ SEQUENCE 160 AA; 17386 MW; 8448FC36594CC958 CRC64;
MNKPLRGAAL AAALAGLVAL EGSETTAYRD IAGVPTICSG TTAGVKMGDK ATPEQCYQMT
IKDFQRFERI VLDAIKVPLN VNEQTALTFF CYNVGPVCTT STAFKRFNQG RATEGCQALA
MWNKVTINGQ KVVSKGLVNR RNAEIKQCLE PSSQYSSLLW
