ID   LYS_BPMS2               Reviewed;          75 AA.
AC   P03609;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Lysis protein;
DE            Short=L protein;
OS   Escherichia phage MS2 (Bacteriophage MS2).
OC   Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC   Levivirales; Leviviridae; Levivirus.
OX   NCBI_TaxID=329852;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   IDENTIFICATION OF PROTEIN CODING REGION.
RX   PubMed=498271; DOI=10.1016/0092-8674(79)90044-8;
RA   Atkins J.F., Steitz J.A., Anderson C.W., Model P.;
RT   "Binding of mammalian ribosomes to MS2 phage RNA reveals an overlapping
RT   gene encoding a lysis function.";
RL   Cell 18:247-256(1979).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-34.
RX   PubMed=4555447; DOI=10.1038/237082a0;
RA   Min Jou W., Haegeman G., Ysebaert M., Fiers W.;
RT   "Nucleotide sequence of the gene coding for the bacteriophage MS2 coat
RT   protein.";
RL   Nature 237:82-88(1972).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-75.
RX   PubMed=1264203; DOI=10.1038/260500a0;
RA   Fiers W., Contreras R., Duerinck F., Haegeman G., Iserentant D.,
RA   Merregaert J., Min Jou W., Molemans F., Raeymaekers A., van den Berghe A.,
RA   Volckaert G., Ysebaert M.;
RT   "Complete nucleotide sequence of bacteriophage MS2 RNA: primary and
RT   secondary structure of the replicase gene.";
RL   Nature 260:500-507(1976).
RN   [4]
RP   INDUCTION.
RX   PubMed=3656424; DOI=10.1016/0022-2836(87)90180-x;
RA   Berkhout B., Schmidt B.F., van Strien A., van Boom J., van Westrenen J.,
RA   van Duin J.;
RT   "Lysis gene of bacteriophage MS2 is activated by translation termination at
RT   the overlapping coat gene.";
RL   J. Mol. Biol. 195:517-524(1987).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=3053640; DOI=10.1128/jb.170.11.5027-5033.1988;
RA   Walderich B., Ursinus-Woessner A., van Duin J., Hoeltje J.V.;
RT   "Induction of the autolytic system of Escherichia coli by specific
RT   insertion of bacteriophage MS2 lysis protein into the bacterial cell
RT   envelope.";
RL   J. Bacteriol. 170:5027-5033(1988).
RN   [6]
RP   FUNCTION.
RX   PubMed=2653958; DOI=10.1016/0378-1097(89)90150-x;
RA   Ursinus-Woessner A., Hoeltje J.V.;
RT   "Functioning of the cloned phage MS2 lysis protein in Escherichia coli
RT   impaired in murein synthesis.";
RL   FEMS Microbiol. Lett. 48:75-79(1989).
RN   [7]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=2656650; DOI=10.1128/jb.171.6.3331-3336.1989;
RA   Walderich B., Hoeltje J.V.;
RT   "Specific localization of the lysis protein of bacteriophage MS2 in
RT   membrane adhesion sites of Escherichia coli.";
RL   J. Bacteriol. 171:3331-3336(1989).
CC   -!- FUNCTION: Induces the formation of specific membrane adhesion sites
CC       between the inner and outer membranes, apparently leading to host cell
CC       lysis. Lysis may be performed via activation of host murein hydrolases.
CC       {ECO:0000269|PubMed:2653958, ECO:0000269|PubMed:2656650}.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane
CC       {ECO:0000269|PubMed:2656650, ECO:0000269|PubMed:3053640}; Single-pass
CC       membrane protein {ECO:0000255}. Host cell outer membrane
CC       {ECO:0000269|PubMed:2656650, ECO:0000269|PubMed:3053640}; Single-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Lysis protein synthesis only occurs when the overlapping
CC       capsid gene is translated. Initiation at the lysis gene is prevented by
CC       a hairpin structure that sequesters the ribosomal binding site. The
CC       ribosome, terminating at the capsid reading frame, covers part of the
CC       lysis hairpin, thereby destabilizing the secondary structure and
CC       allowing the reading of the lysis gene. {ECO:0000269|PubMed:3656424}.
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DR   EMBL; V00642; CAA23990.1; -; mRNA.
DR   PIR; A90787; YVBPMS.
DR   RefSeq; NP_040649.1; NC_001417.2.
DR   Proteomes; UP000002127; 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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR022599; Phage_MS2_lysis.
DR   Pfam; PF11125; DUF2830; 1.
PE   2: Evidence at transcript level;
KW   Cytolysis; Host cell inner membrane; Host cell lysis by virus;
KW   Host cell membrane; Host cell outer membrane; Host membrane; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Viral release from host cell.
FT   CHAIN           1..75
FT                   /note="Lysis protein"
FT                   /id="PRO_0000164864"
FT   TRANSMEM        38..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   75 AA;  8870 MW;  643FBA689F4D436F CRC64;
     METRFPQQSQ QTPASTNRRR PFKHEDYPCR RQQRSSTLYV LIFLAIFLSK FTNQLLLSLL
     EAVIRTVTTL QQLLT