TERS_BPP22
ID TERS_BPP22 Reviewed; 162 AA.
AC P04893; Q7PCC9;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 93.
DE RecName: Full=Terminase, small subunit {ECO:0000303|PubMed:18775728};
DE AltName: Full=DNA-packaging protein gp3 {ECO:0000305};
GN Name=3;
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].
RX PubMed=2991569; DOI=10.1128/jvi.55.2.458-465.1985;
RA Backhaus H.;
RT "DNA packaging initiation of Salmonella bacteriophage P22: determination of
RT cut sites within the DNA sequence coding for gene 3.";
RL J. Virol. 55:458-465(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-7.
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 [3]
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 [4]
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 [5]
RP INTERACTION WITH THE TERMINASE SMALL SUBUNIT, SUBUNIT, AND MUTAGENESIS OF
RP ALA-112.
RX PubMed=17945256; DOI=10.1016/j.jmb.2007.08.070;
RA Nemecek D., Gilcrease E.B., Kang S., Prevelige P.E. Jr., Casjens S.,
RA Thomas G.J. Jr.;
RT "Subunit conformations and assembly states of a DNA-translocating motor:
RT the terminase of bacteriophage P22.";
RL J. Mol. Biol. 374:817-836(2007).
RN [6]
RP SUBUNIT, DNA-BINDING, AND FUNCTION.
RX PubMed=18775728; DOI=10.1016/j.jmb.2008.08.050;
RA Nemecek D., Lander G.C., Johnson J.E., Casjens S.R., Thomas G.J. Jr.;
RT "Assembly architecture and DNA binding of the bacteriophage P22 terminase
RT small subunit.";
RL J. Mol. Biol. 383:494-501(2008).
RN [7]
RP SUBUNIT.
RX PubMed=21206037; DOI=10.1107/s174430911004697x;
RA Roy A., Bhardwaj A., Cingolani G.;
RT "Crystallization of the nonameric small terminase subunit of bacteriophage
RT P22.";
RL Acta Crystallogr. F 67:104-110(2011).
RN [8]
RP INTERACTION WITH THE TERMINASE LARGE SUBUNIT, AND SUBUNIT.
RX PubMed=26301600; DOI=10.1016/j.jmb.2015.08.013;
RA McNulty R., Lokareddy R.K., Roy A., Yang Y., Lander G., Heck A.J.,
RA Johnson J.E., Cingolani G.;
RT "Architecture of the Complex Formed by Large and Small Terminase Subunits
RT from Bacteriophage P22.";
RL J. Mol. Biol. 427:3285-3299(2015).
RN [9] {ECO:0007744|PDB:3P9A}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND FUNCTION.
RX PubMed=22771211; DOI=10.1016/j.str.2012.05.014;
RA Roy A., Bhardwaj A., Datta P., Lander G.C., Cingolani G.;
RT "Small terminase couples viral DNA binding to genome-packaging ATPase
RT activity.";
RL Structure 20:1403-1413(2012).
CC -!- FUNCTION: The terminase small subunit binds to the packaging initiation
CC site and regulates the ATPase activity of the terminase large subunit.
CC The terminase lies at a unique vertex of the procapsid and is composed
CC of two subunits, a small terminase subunit involved in viral DNA
CC recognition (packaging sequence), and a large terminase subunit
CC possessing endonucleolytic and ATPase activities. Both terminase
CC subunits heterooligomerize and are docked on the portal protein to form
CC the packaging machine. The terminase large subunit exhibits
CC endonuclease activity and cleaves the viral genome concatemer once the
CC capsid is full (headful packaging). Once the capsid is packaged with
CC the DNA, the terminase complex is substituted by neck proteins.
CC {ECO:0000305|PubMed:18775728}.
CC -!- SUBUNIT: Homononamer; forms a ring-like structure through which genomic
CC DNA is translocated into the capsid. Interacts with the terminase large
CC subunit; the active complex is composed of a monomer of the terminase
CC large subunit and a nonamer ring of terminase small subunits.
CC {ECO:0000269|PubMed:17945256, ECO:0000269|PubMed:18775728,
CC ECO:0000269|PubMed:21206037, ECO:0000269|PubMed:26301600}.
CC -!- INTERACTION:
CC P04893; P04893: 3; NbExp=3; IntAct=EBI-15994787, EBI-15994787;
CC -!- SIMILARITY: Belongs to the P22likvirus small terminase family.
CC {ECO:0000305}.
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DR EMBL; M10075; AAA32272.1; -; Genomic_DNA.
DR EMBL; M59749; AAA72958.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75043.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA01046.1; -; Genomic_DNA.
DR PIR; A04292; Z3BP22.
DR RefSeq; YP_063714.1; NC_002371.2.
DR PDB; 3P9A; X-ray; 1.76 A; A/B/C/D/E/F/G/H/I=1-162.
DR PDBsum; 3P9A; -.
DR SMR; P04893; -.
DR DIP; DIP-59855N; -.
DR IntAct; P04893; 1.
DR GeneID; 2944227; -.
DR KEGG; vg:2944227; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; Genome.
DR GO; GO:0043493; C:viral terminase complex; IDA:UniProtKB.
DR GO; GO:0097710; C:viral terminase, small subunit; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR InterPro; IPR032066; GP3_package.
DR Pfam; PF16677; GP3_package; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Late protein;
KW Reference proteome; Viral genome packaging; Viral release from host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:1853558"
FT CHAIN 2..162
FT /note="Terminase, small subunit"
FT /id="PRO_0000077744"
FT DNA_BIND 143..152
FT /evidence="ECO:0000269|PubMed:18775728"
FT REGION 132..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..162
FT /note="Interaction with the terminase large subunit gp2"
FT /evidence="ECO:0000269|PubMed:26301600"
FT MUTAGEN 112
FT /note="A->T: Loss of self assembly as a homononamer, but
FT homodecamer instead. Retardation of the rate of ring
FT formation."
FT /evidence="ECO:0000269|PubMed:17945256"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3P9A"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:3P9A"
FT STRAND 44..54
FT /evidence="ECO:0007829|PDB:3P9A"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3P9A"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:3P9A"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:3P9A"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3P9A"
FT HELIX 90..112
FT /evidence="ECO:0007829|PDB:3P9A"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:3P9A"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3P9A"
SQ SEQUENCE 162 AA; 18650 MW; C2762E20C1FDDBB7 CRC64;
MAAPKGNRFW EARSSHGRNP KFESPEALWA ACCEYFEWVE ANPLWEMKAF SYQGEVIQEP
IAKMRAMTIT GLTLFIDVTL ETWRTYRLRE DLSEVVTRAE QVIYDQKFSG AAADLLNANI
IARDLGLKEQ SQVEDVTPDK GDRDKRRSRI KELFNRGTGR DS
