ID   EXLYS_BPAPS             Reviewed;         160 AA.
AC   Q9T1S1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Peptidoglycan hydrolase gp27;
DE   AltName: Full=Gene product 27;
DE            Short=Gp27;
DE   AltName: Full=Internal virion protein gp27;
GN   Name=27;
OS   Acyrthosiphon pisum secondary endosymbiont phage 1 (Bacteriophage APSE-1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Sendosyvirus.
OX   NCBI_TaxID=2682836;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10489345; DOI=10.1006/viro.1999.9902;
RA   van der Wilk F., Dullemans A.M., Verbeek M., van den Heuvel J.F.J.M.;
RT   "Isolation and characterization of APSE-1, a bacteriophage infecting the
RT   secondary endosymbiont of acyrthosiphon pisum.";
RL   Virology 262:104-113(1999).
CC   -!- FUNCTION: Component of the cylindrical core that assembles on the inner
CC       surface of the capsid during procapsid formation. Required for
CC       stabilization of the condensed DNA within the capsid; perhaps by
CC       plugging the hole through which the DNA enters. Plays a role in
CC       ejection of the bacteriophage DNA into the host cell at the initiation
CC       of infection. Functions as an exolysin that catalyzes the cleavage of
CC       the glycosidic bonds between N-acetylmuramic acid and N-
CC       acetylglucosamine residues in peptidoglycans.
CC       {ECO:0000250|UniProtKB:P26746}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P26746}.
CC   -!- SIMILARITY: To phage P22 gp4. {ECO:0000305}.
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DR   EMBL; AF157835; AAF03970.1; -; Genomic_DNA.
DR   RefSeq; NP_050988.1; NC_000935.1.
DR   SMR; Q9T1S1; -.
DR   GeneID; 1262321; -.
DR   KEGG; vg:1262321; -.
DR   Proteomes; UP000000853; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-KW.
DR   GO; GO:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3230.20; -; 1.
DR   InterPro; IPR038258; Gp4_sf.
DR   InterPro; IPR020362; Tail_accessory_Gp4.
DR   Pfam; PF11650; P22_Tail-4; 1.
PE   3: Inferred from homology;
KW   Degradation of host cell envelope components during virus entry;
KW   Degradation of host peptidoglycans during virus entry; Hydrolase;
KW   Late protein; Reference proteome;
KW   Viral genome ejection through host cell envelope;
KW   Viral penetration into host cytoplasm; Viral short tail ejection system;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..160
FT                   /note="Peptidoglycan hydrolase gp27"
FT                   /id="PRO_0000077751"
SQ   SEQUENCE   160 AA;  17449 MW;  EE92835135B8A65F CRC64;
     MTKPLTKGEI VLFALRKAGI ASEATNIDVE PQSFEEGIND LEDLMAELQI TFGDLGYQFS
     AEEENPTSDD ASGLPRKYKQ VMGYQLMLRM LSDYGIEPTP RQEASAAAAY DALLTDTLSV
     PSIARRGDMP VGQGNNYTAL GTASYYVERG FHAKNTDPVS