EXLYS_BPPH6
ID EXLYS_BPPH6 Reviewed; 220 AA.
AC P07582; Q38459;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 29-SEP-2021, entry version 68.
DE RecName: Full=Peptidoglycan hydrolase gp5 {ECO:0000305};
DE AltName: Full=Gene product 5 {ECO:0000305};
DE Short=Gp5;
GN Name=P5; Synonyms=P11;
OS Pseudomonas phage phi6 (Bacteriophage phi-6).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Vidaverviricetes;
OC Mindivirales; Cystoviridae; Cystovirus.
OX NCBI_TaxID=10879;
OH NCBI_TaxID=319; Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. phaseolicola).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3754015; DOI=10.1128/jvi.58.1.142-151.1986;
RA McGraw T., Mindich L., Frangione B.;
RT "Nucleotide sequence of the small double-stranded RNA segment of
RT bacteriophage phi 6: novel mechanism of natural translational control.";
RL J. Virol. 58:142-151(1986).
RN [2]
RP FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1390911; DOI=10.1016/0167-4838(92)90073-m;
RA Caldentey J., Bamford D.H.;
RT "The lytic enzyme of the Pseudomonas phage phi 6. Purification and
RT biochemical characterization.";
RL Biochim. Biophys. Acta 1159:44-50(1992).
RN [3]
RP REVIEW.
RX PubMed=22991936; DOI=10.3109/1040841x.2012.723675;
RA Rodriguez-Rubio L., Martinez B., Donovan D.M., Rodriguez A., Garcia P.;
RT "Bacteriophage virion-associated peptidoglycan hydrolases: potential new
RT enzybiotics.";
RL Crit. Rev. Microbiol. 39:427-434(2013).
CC -!- FUNCTION: Muralytic enzyme exposed to host peptidoglycan layer after
CC membrane fusion during viral entry. Functions as an exolysin that
CC cleaves the peptide bridge formed by meso-diaminopimelic acid and D-
CC alanine. Also lyses the host cell late in infection to release the
CC virions. {ECO:0000269|PubMed:1390911}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:1390911};
CC Temperature dependence:
CC Inactivated at temperatures above 20 degrees Celsius.
CC {ECO:0000269|PubMed:1390911};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1390911}.
CC -!- SUBCELLULAR LOCATION: Virion. Note=Located between the capsid and the
CC envelope.
CC -!- SIMILARITY: Belongs to the peptidase U40 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Val-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32362.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M12921; AAA32361.1; -; Genomic_RNA.
DR EMBL; M12921; AAA32362.1; ALT_INIT; Genomic_RNA.
DR PIR; D23368; YVBPF6.
DR RefSeq; NP_620343.1; NC_003714.1.
DR RefSeq; NP_620344.1; NC_003714.1.
DR SMR; P07582; -.
DR MEROPS; U40.001; -.
DR GeneID; 956433; -.
DR GeneID; 956434; -.
DR KEGG; vg:956433; -.
DR KEGG; vg:956434; -.
DR Proteomes; UP000002610; Genome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; 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:0044409; P:entry into host; IDA:UniProtKB.
DR Gene3D; 1.10.530.50; -; 1.
DR InterPro; IPR038288; Gp5_sf.
DR InterPro; IPR019505; Peptidase_U40.
DR Pfam; PF10464; Peptidase_U40; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Degradation of host cell envelope components during virus entry;
KW Degradation of host peptidoglycans during virus entry;
KW Host cell lysis by virus; Hydrolase; Reference proteome;
KW Viral release from host cell; Virion; Virus entry into host cell.
FT CHAIN 1..220
FT /note="Peptidoglycan hydrolase gp5"
FT /id="PRO_0000164636"
SQ SEQUENCE 220 AA; 24149 MW; 28BA74411370823D CRC64;
MSKDSAFAVQ YSLRALGQKV RADGVVGSET RAALDALPEN QKKAIVELQA LLPKAQSVGN
NRVRFTTAEV DSAVARISQK IGVPASYYQF LIPIENFVVA GGFETTVSGS FRGLGQFNRQ
TWDRLRRLGR NLPAFEEGSA QLNASLYAIG FLYLENKRAY EASFKGRVFT HEIAYLYHNQ
GAPAAEQYLT SGRLVYPKQS EAAVAAVAAA RNQHVKESWA