LYS_BPPHS
ID LYS_BPPHS Reviewed; 91 AA.
AC P03639;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Lysis protein E;
DE Short=Protein E;
DE AltName: Full=GPE;
GN Name=E;
OS Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174).
OC Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC Petitvirales; Microviridae; Bullavirinae; Sinsheimervirus.
OX NCBI_TaxID=1217068;
OH NCBI_TaxID=498388; Escherichia coli C.
RN [1] {ECO:0000312|EMBL:AAA32576.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=870828; DOI=10.1038/265687a0;
RA Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C.,
RA Hutchison C.A. III, Slocombe P.M., Smith M.;
RT "Nucleotide sequence of bacteriophage phi X174 DNA.";
RL Nature 265:687-695(1977).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1004533; DOI=10.1038/264034a0;
RA Barrell B.G., Air G.M., Hutchison C.A. III;
RT "Overlapping genes in bacteriophage phiX174.";
RL Nature 264:34-41(1976).
RN [3] {ECO:0000312|EMBL:CAA84691.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7867948; DOI=10.1016/0378-1119(94)00839-k;
RA Henrich B., Schmidtberger B.;
RT "Positive-selection vector with enhanced lytic potential based on a variant
RT of phi X174 phage gene E.";
RL Gene 154:51-54(1995).
RN [4]
RP OLIGOMERIZATION.
RX PubMed=2466836; DOI=10.1016/s0021-9258(18)83778-4;
RA Blasi U., Linke R.P., Lubitz W.;
RT "Evidence for membrane-bound oligomerization of bacteriophage phi X174
RT lysis protein-E.";
RL J. Biol. Chem. 264:4552-4558(1989).
RN [5]
RP MUTAGENESIS OF PRO-21.
RX PubMed=9383158; DOI=10.1046/j.1365-2958.1997.5781941.x;
RA Witte A., Schrot G., Schon P., Lubitz W.;
RT "Proline 21, a residue within the alpha-helical domain of phiX174 lysis
RT protein E, is required for its function in Escherichia coli.";
RL Mol. Microbiol. 26:337-346(1997).
RN [6]
RP FUNCTION.
RX PubMed=10760296; DOI=10.1073/pnas.97.8.4297;
RA Bernhardt T.G., Roof W.D., Young R.;
RT "Genetic evidence that the bacteriophage phi X174 lysis protein inhibits
RT cell wall synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4297-4302(2000).
RN [7]
RP FUNCTION.
RX PubMed=11078734; DOI=10.1074/jbc.m007638200;
RA Bernhardt T.G., Struck D.K., Young R.;
RT "The lysis protein E of phi X174 is a specific inhibitor of the MraY-
RT catalyzed step in peptidoglycan synthesis.";
RL J. Biol. Chem. 276:6093-6097(2001).
RN [8]
RP INTERACTION WITH HOST SLYD AND MRAY.
RX PubMed=17005977; DOI=10.1099/mic.0.28776-0;
RA Mendel S., Holbourn J.M., Schouten J.A., Bugg T.D.;
RT "Interaction of the transmembrane domain of lysis protein E from
RT bacteriophage phiX174 with bacterial translocase MraY and peptidyl-prolyl
RT isomerase SlyD.";
RL Microbiology 152:2959-2967(2006).
RN [9]
RP FUNCTION.
RX PubMed=19379010; DOI=10.1021/bi900469g;
RA Zheng Y., Struck D.K., Young R.;
RT "Purification and functional characterization of phiX174 lysis protein E.";
RL Biochemistry 48:4999-5006(2009).
RN [10]
RP INTERACTION WITH HOST MRAY.
RX PubMed=22742425; DOI=10.1111/j.1365-2958.2012.08153.x;
RA Tanaka S., Clemons W.M. Jr.;
RT "Minimal requirements for inhibition of MraY by lysis protein E from
RT bacteriophage PhiX174.";
RL Mol. Microbiol. 85:975-985(2012).
CC -!- FUNCTION: Induces host cell lysis. Inhibits the host translocase MraY
CC activity that catalyzes the synthesis of lipid I, a necessary step for
CC the host cell wall biosynthesis. {ECO:0000269|PubMed:10760296,
CC ECO:0000269|PubMed:11078734, ECO:0000269|PubMed:19379010}.
CC -!- SUBUNIT: Oligomerizes. Interacts (via N-terminal) with host SlyD; this
CC interaction supposely protects E from proteolysis and therefore allows
CC E to interact with and inhibit host MraY at the host membrane
CC (PubMed:17005977). Interacts with host MraY; this interaction inhibits
CC MraY translocase activity (PubMed:22742425).
CC {ECO:0000269|PubMed:17005977, ECO:0000269|PubMed:22742425}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Most of the references in this paper show that residue
CC 89 is Arg, in most other phiX174 proteomes the residue is Gln. We have
CC chosen to show Gln at this position. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the microvirus E protein family. {ECO:0000305}.
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DR EMBL; J02482; AAA32576.1; -; Genomic_DNA.
DR EMBL; Z35638; CAA84691.1; -; Genomic_DNA.
DR PIR; A04247; ZEBPF4.
DR TCDB; 1.C.129.1.1; the Phix174 lysis protein e (Phix174-e or phix174-e) family.
DR Proteomes; UP000005893; 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:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0039635; P:suppression by virus of host peptidoglycan biosynthetic process; IDA:CACAO.
DR GO; GO:0039640; P:viral release by cytolysis via suppression of host peptidoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:CACAO.
DR InterPro; IPR007605; Micrvir_lysisE.
DR Pfam; PF04517; Microvir_lysis; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Host cell lysis by virus; Host cell membrane; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral release from host cell.
FT CHAIN 1..91
FT /note="Lysis protein E"
FT /id="PRO_0000164885"
FT TOPO_DOM 1..8
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MUTAGEN 21
FT /note="P->A: Loss of E-mediated host lysis."
FT /evidence="ECO:0000269|PubMed:9383158"
FT MUTAGEN 21
FT /note="P->G: Loss of E-mediated host lysis."
FT /evidence="ECO:0000269|PubMed:9383158"
FT MUTAGEN 21
FT /note="P->S: Loss of E-mediated host lysis."
FT /evidence="ECO:0000269|PubMed:9383158"
FT MUTAGEN 21
FT /note="P->V: Loss of E-mediated host lysis."
FT /evidence="ECO:0000269|PubMed:9383158"
FT CONFLICT 89
FT /note="Q -> R (in Ref. 1; AAA32576 and 2; no nucleotide
FT entry)"
SQ SEQUENCE 91 AA; 10574 MW; F44DB400197D829A CRC64;
MVRWTLWDTL AFLLLLSLLL PSLLIMFIPS TFKRPVSSWK ALNLRKTLLM ASSVRLKPLN
CSRLPCVYAQ ETLTFLLTQK KTCVKNYVQK E
