ID   EXLYS_BPPM2             Reviewed;          34 AA.
AC   Q9XJR8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   29-SEP-2021, entry version 49.
DE   RecName: Full=Peptidoglycan hydrolase P7;
DE   AltName: Full=Protein VII;
GN   Name=VII;
OS   Pseudoalteromonas phage PM2 (Bacteriophage PM2).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Vinavirales; Corticoviridae; Corticovirus.
OX   NCBI_TaxID=10661;
OH   NCBI_TaxID=28107; Pseudoalteromonas espejiana.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10502514; DOI=10.1006/viro.1999.9837;
RA   Maennistoe R.H., Kivelae H.M., Paulin L., Bamford D.H., Bamford J.K.;
RT   "The complete genome sequence of PM2, the first lipid-containing bacterial
RT   virus to be isolated.";
RL   Virology 262:355-363(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10.
RX   PubMed=10502515; DOI=10.1006/viro.1999.9838;
RA   Kivelae H.M., Maennistoe R.H., Kalkkinen N., Bamford D.H.;
RT   "Purification and protein composition of PM2, the first lipid-containing
RT   bacterial virus to be isolated.";
RL   Virology 262:364-374(1999).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-7, AND SUBCELLULAR LOCATION.
RX   PubMed=12134022; DOI=10.1128/jvi.76.16.8169-8178.2002;
RA   Kivelae H.M., Kalkkinen N., Bamford D.H.;
RT   "Bacteriophage PM2 has a protein capsid surrounding a spherical
RT   proteinaceous lipid core.";
RL   J. Virol. 76:8169-8178(2002).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-8, AND FUNCTION.
RX   PubMed=15292135; DOI=10.1128/jb.186.16.5342-5354.2004;
RA   Kivelae H.M., Daugelavicius R., Hankkio R.H., Bamford J.K., Bamford D.H.;
RT   "Penetration of membrane-containing double-stranded-DNA bacteriophage PM2
RT   into Pseudoalteromonas hosts.";
RL   J. Bacteriol. 186:5342-5354(2004).
CC   -!- FUNCTION: Exolysin that catalyzes the cleavage of the host
CC       peptidoglycans during virus entry. {ECO:0000269|PubMed:15292135}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:12134022};
CC       Single-pass membrane protein {ECO:0000305|PubMed:12134022}. Note=Part
CC       of the capsid inner membrane. {ECO:0000305}.
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DR   EMBL; AF155037; AAD43548.1; -; Genomic_DNA.
DR   RefSeq; NP_049902.1; NC_000867.1.
DR   SMR; Q9XJR8; -.
DR   GeneID; 1262042; -.
DR   KEGG; vg:1262042; -.
DR   Proteomes; UP000002136; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039641; C:viral inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IDA:CACAO.
DR   GO; GO:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Capsid inner membrane protein;
KW   Degradation of host cell envelope components during virus entry;
KW   Degradation of host peptidoglycans during virus entry;
KW   Direct protein sequencing; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Virion; Virus entry into host cell.
FT   CHAIN           1..34
FT                   /note="Peptidoglycan hydrolase P7"
FT                   /id="PRO_0000339904"
FT   TRANSMEM        10..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   34 AA;  3653 MW;  EB0F87FE984240F3 CRC64;
     MINKTTIKTV LITLGVLAAV NKVSALRSVK RLIS