EXLYS_BPP22
ID EXLYS_BPP22 Reviewed; 166 AA.
AC P26746; Q7PCI3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 02-JUN-2021, entry version 85.
DE RecName: Full=Peptidoglycan hydrolase gp4;
DE AltName: Full=Gene product 4;
DE Short=Gp4;
DE AltName: Full=Internal virion protein gp4;
DE AltName: Full=Tail adapter protein gp4;
GN Name=4;
OS Salmonella phage P22 (Bacteriophage P22).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10754;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-17.
RX PubMed=1853558; DOI=10.1016/0042-6822(91)90981-g;
RA Eppler K., Wyckoff E., Goates J., Parr R., Casjens S.;
RT "Nucleotide sequence of the bacteriophage P22 genes required for DNA
RT packaging.";
RL Virology 183:519-538(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA Vander Byl C.S., Kropinski A.M.B.;
RT "Sequence of the genome of Salmonella bacteriophage P22.";
RL J. Bacteriol. 182:6472-6481(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA Casjens S.R.;
RT "Corrected sequence of the bacteriophage P22 genome.";
RL J. Bacteriol. 185:1475-1477(2003).
RN [4]
RP FUNCTION, AND PROTEIN SEQUENCE OF 1-14.
RX PubMed=14763988; DOI=10.1046/j.1365-2958.2003.03894.x;
RA Moak M., Molineux I.J.;
RT "Peptidoglycan hydrolytic activities associated with bacteriophage
RT virions.";
RL Mol. Microbiol. 51:1169-1183(2004).
RN [5]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH THE PORTAL PROTEIN.
RX PubMed=16970964; DOI=10.1016/j.jmb.2006.08.014;
RA Olia A.S., Al-Bassam J., Winn-Stapley D.A., Joss L., Casjens S.R.,
RA Cingolani G.;
RT "Binding-induced stabilization and assembly of the phage P22 tail accessory
RT factor gp4.";
RL J. Mol. Biol. 363:558-576(2006).
RN [6]
RP INTERACTION WITH THE PORTAL PROTEIN.
RX PubMed=28134243; DOI=10.1038/ncomms14310;
RA Lokareddy R.K., Sankhala R.S., Roy A., Afonine P.V., Motwani T.,
RA Teschke C.M., Parent K.N., Cingolani G.;
RT "Portal protein functions akin to a DNA-sensor that couples genome-
RT packaging to icosahedral capsid maturation.";
RL Nat. Commun. 8:14310-14310(2017).
RN [7] {ECO:0007744|PDB:4V4K}
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).
RX PubMed=21499245; DOI=10.1038/nsmb.2023;
RA Olia A.S., Prevelige P.E. Jr., Johnson J.E., Cingolani G.;
RT "Three-dimensional structure of a viral genome-delivery portal vertex.";
RL Nat. Struct. Mol. Biol. 18:597-603(2011).
CC -!- FUNCTION: Tail protein located at the vertex occupied by the portal
CC ring. 12 copies of gp4 form a structural ring at the bottom of the
CC portal ring. Together with gp10 and gp26, gp4 is required for
CC stabilization of the condensed DNA within the capsid; perhaps by
CC plugging the hole through which the DNA enters. Probably functions as a
CC head completion protein. Plays a role in ejection of the bacteriophage
CC DNA into the host cell at the initiation of infection. Functions as an
CC exolysin that catalyzes the cleavage of the glycosidic bonds between N-
CC acetylmuramic acid and N-acetylglucosamine residues in peptidoglycans.
CC {ECO:0000269|PubMed:14763988, ECO:0000269|PubMed:16970964,
CC ECO:0000269|PubMed:21499245}.
CC -!- SUBUNIT: Monomer; homododecamer upon binding to the portal ring
CC (PubMed:16970964). Interacts (via C-terminus) with the portal protein;
CC this interaction participates in the head completion (PubMed:28134243,
CC PubMed:16970964). {ECO:0000269|PubMed:28134243}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- DOMAIN: The N-terminus changes its conformation when transitioning from
CC the preassembly state to the postassembly state.
CC {ECO:0000250|UniProtKB:Q716G8}.
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DR EMBL; M59749; AAA72964.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75049.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA00989.1; -; Genomic_DNA.
DR PIR; F40474; Z4BP22.
DR RefSeq; NP_059632.1; NC_002371.2.
DR PDB; 4V4K; X-ray; 3.25 A; Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v=1-166.
DR PDB; 5GAI; EM; 10.50 A; K/L/M/N/O/P/Q/R/S/T/U/V=5-150.
DR PDBsum; 4V4K; -.
DR PDBsum; 5GAI; -.
DR SMR; P26746; -.
DR DIP; DIP-59582N; -.
DR IntAct; P26746; 1.
DR GeneID; 1262828; -.
DR KEGG; vg:1262828; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; Genome.
DR GO; GO:0098015; C:virus tail; IDA:CACAO.
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; IDA:UniProtKB.
DR GO; GO:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure;
KW Degradation of host cell envelope components during virus entry;
KW Degradation of host peptidoglycans during virus entry;
KW Direct protein sequencing; Hydrolase; 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..166
FT /note="Peptidoglycan hydrolase gp4"
FT /id="PRO_0000077750"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4V4K"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:4V4K"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4V4K"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4V4K"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4V4K"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4V4K"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:4V4K"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:4V4K"
FT HELIX 101..121
FT /evidence="ECO:0007829|PDB:4V4K"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4V4K"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:4V4K"
SQ SEQUENCE 166 AA; 18025 MW; 4CAEAD9529C9C502 CRC64;
MQIKTKGDLV RAALRKLGVA SDATLTDVEP QSMQDAVDDL EAMMAEWYQD GKGIITGYVF
SDDENPPAEG DDHGLRSSAV SAVFHNLACR IAPDYALEAT AKIIATAKYG KELLYKQTAI
SRAKRAPYPS RMPTGSGNSF ANLNEWHYFP GEQNADSTTP HDEGNG
