SPAC_BPT4
ID SPAC_BPT4 Reviewed; 97 AA.
AC P39230;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein spackle {ECO:0000255|HAMAP-Rule:MF_04159};
DE Flags: Precursor;
GN Name=sp {ECO:0000255|HAMAP-Rule:MF_04159}; Synonyms=61.3;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383243; DOI=10.1128/jvi.67.4.2305-2316.1993;
RA Selick H.E., Stormo G.D., Dyson R.L., Alberts B.M.;
RT "Analysis of five presumptive protein-coding sequences clustered between
RT the primosome genes, 41 and 61, of bacteriophages T4, T2, and T6.";
RL J. Virol. 67:2305-2316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP IDENTIFICATION.
RX PubMed=10417260; DOI=10.1006/viro.1999.9829;
RA Kai T., Ueno H., Otsuka Y., Morimoto W., Yonesaki T.;
RT "Gene 61.3 of bacteriophage T4 is the spackle gene.";
RL Virology 260:254-259(1999).
RN [4]
RP FUNCTION.
RX PubMed=4589853; DOI=10.1128/jvi.13.2.312-321.1974;
RA Cornett J.B.;
RT "Spackle and immunity functions of bacteriophage T4.";
RL J. Virol. 13:312-321(1974).
RN [5] {ECO:0007744|PDB:6X6O}
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS), SUBUNIT, AND DISULFIDE BOND.
RX PubMed=32876065; DOI=10.1107/s2059798320010979;
RA Shi K., Kurniawan F., Banerjee S., Moeller N.H., Aihara H.;
RT "Crystal structure of bacteriophage T4 Spackle as determined by native SAD
RT phasing.";
RL Acta Crystallogr. D 76:899-904(2020).
RN [6] {ECO:0007744|PDB:6XC0, ECO:0007744|PDB:6XC1}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS), INTERACTION WITH THE BASEPLATE
RP CENTRAL SPIKE PROTEIN GP5, AND FUNCTION.
RX PubMed=33214665; DOI=10.1038/s42003-020-01412-3;
RA Shi K., Oakland J.T., Kurniawan F., Moeller N.H., Banerjee S., Aihara H.;
RT "Structural basis of superinfection exclusion by bacteriophage T4
RT Spackle.";
RL Commun. Biol. 3:691-691(2020).
RN [7] {ECO:0007744|PDB:7CN6, ECO:0007744|PDB:7CN7}
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 23-97, SUBCELLULAR LOCATION,
RP INTERACTION WITH THE BASEPLATE CENTRAL SPIKE PROTEIN GP5, AND FUNCTION.
RX PubMed=32987925; DOI=10.3390/v12101070;
RA Kanamaru S., Uchida K., Nemoto M., Fraser A., Arisaka F., Leiman P.G.;
RT "Structure and Function of the T4 Spackle Protein Gp61.3.";
RL Viruses 12:0-0(2020).
CC -!- FUNCTION: Inhibits viral DNA ejection into the host cytoplasm, thereby
CC confering the infected host bacteria with immunity against secondary
CC phage infection (PubMed:4589853). Achieves superinfection exclusion by
CC localizing to the periplasm and inhibiting the activity of tail-
CC associated lysozyme, thereby preventing penetration by the tail tube of
CC incoming phages (PubMed:32987925, PubMed:33214665). {ECO:0000255|HAMAP-
CC Rule:MF_04159, ECO:0000269|PubMed:32987925,
CC ECO:0000269|PubMed:33214665, ECO:0000269|PubMed:4589853}.
CC -!- SUBUNIT: Monomer (PubMed:32876065). Interacts with the baseplate
CC central spike protein Gp5; this interaction selectively inhibits the
CC lysozyme activity of the baseplate central spike protein
CC (PubMed:32987925, PubMed:33214665). {ECO:0000255|HAMAP-Rule:MF_04159,
CC ECO:0000269|PubMed:32876065, ECO:0000269|PubMed:32987925,
CC ECO:0000269|PubMed:33214665}.
CC -!- SUBCELLULAR LOCATION: Host periplasm {ECO:0000255|HAMAP-Rule:MF_04159,
CC ECO:0000269|PubMed:32987925}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae spackle protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04159}.
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DR EMBL; S57514; AAB25710.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42510.1; -; Genomic_DNA.
DR PIR; C45681; C45681.
DR RefSeq; NP_049651.1; NC_000866.4.
DR PDB; 6X6O; X-ray; 1.52 A; A/B=1-97.
DR PDB; 6XC0; X-ray; 1.78 A; C/D=1-97.
DR PDB; 6XC1; X-ray; 1.92 A; C=1-97.
DR PDB; 7CN6; X-ray; 1.60 A; A/B/C=23-97.
DR PDB; 7CN7; X-ray; 1.15 A; C=23-97.
DR PDBsum; 6X6O; -.
DR PDBsum; 6XC0; -.
DR PDBsum; 6XC1; -.
DR PDBsum; 7CN6; -.
DR PDBsum; 7CN7; -.
DR SMR; P39230; -.
DR GeneID; 1258657; -.
DR KEGG; vg:1258657; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0044229; C:host cell periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0098669; P:superinfection exclusion; IDA:UniProtKB.
DR HAMAP; MF_04159; SPACKLE_T4; 1.
DR InterPro; IPR046391; SPACKLE_T4.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Host periplasm; Host-virus interaction;
KW Reference proteome; Signal; Superinfection exclusion.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04159"
FT CHAIN 23..97
FT /note="Protein spackle"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04159"
FT /id="PRO_0000003330"
FT DISULFID 29..81
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04159,
FT ECO:0000269|PubMed:32876065"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 37..55
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:7CN7"
SQ SEQUENCE 97 AA; 10994 MW; E0A5E5E076C97965 CRC64;
MKKFIFATIF ALASCAAQPA MAGYDKDLCE WSMTADQTEV ETQIEADIMN IVKRDRPEMK
AEVQKQLKSG GVMQYNYVLY CDKNFNNKNI IAEVVGE
