TERS_BPSF6
ID TERS_BPSF6 Reviewed; 145 AA.
AC P68928; Q1EJR8; Q38627;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Terminase small subunit;
DE AltName: Full=G1P;
DE AltName: Full=Terminase, small subunit;
GN Name=1;
OS Bacillus phage SF6 (Bacteriophage SF6).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=10773;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX PubMed=8030254; DOI=10.1006/viro.1994.1415;
RA Chai S., Kruft V., Alonso J.C.;
RT "Analysis of the Bacillus subtilis bacteriophages SPP1 and SF6 gene 1
RT product: a protein involved in the initiation of headful packaging.";
RL Virology 202:930-939(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Benini S., Chechik M., Ortiz-Lombardia M., Polier S., Shevtsov M.B.,
RA De Luchi D., Alonso J.C., Antson A.A.;
RT "The DNA-binding domain of bacteriophage SF6 small terminase subunit.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:3ZQM, ECO:0007744|PDB:3ZQN, ECO:0007744|PDB:3ZQO, ECO:0007744|PDB:3ZQP, ECO:0007744|PDB:3ZQQ}
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 53-120, AND SUBUNIT.
RX PubMed=22207627; DOI=10.1073/pnas.1110270109;
RA Buttner C.R., Chechik M., Ortiz-Lombardia M., Smits C., Ebong I.O.,
RA Chechik V., Jeschke G., Dykeman E., Benini S., Robinson C.V., Alonso J.C.,
RA Antson A.A.;
RT "Structural basis for DNA recognition and loading into a viral packaging
RT motor.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:811-816(2012).
RN [4] {ECO:0007744|PDB:2CMP}
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1-60, AND DNA-BINDING.
RX PubMed=23545641; DOI=10.1107/s1744309113004399;
RA Benini S., Chechik M., Ortiz Lombardia M., Polier S., Leech A.,
RA Shevtsov M.B., Alonso J.C.;
RT "The 1.58 A resolution structure of the DNA-binding domain of bacteriophage
RT SF6 small terminase provides new hints on DNA binding.";
RL Acta Crystallogr. F 69:376-381(2013).
CC -!- FUNCTION: The terminase small subunit specifically recognizes the non-
CC adjacent pacL and pacR packaging subsites and regulates the ATPase
CC activity of the terminase large subunit. The terminase lies at a unique
CC vertex of the procapsid and is composed of two subunits, a small
CC terminase subunit involved in viral DNA recognition (packaging
CC sequence), and a large terminase subunit possessing endonucleolytic and
CC ATPase activities. Both terminase subunits heterooligomerize and are
CC docked on the portal protein to form the packaging machine. The
CC terminase large subunit exhibits endonuclease activity and cleaves the
CC viral genome concatemer once the capsid is full (headful packaging).
CC Once the capsid is packaged with the DNA, the terminase complex is
CC substituted by neck proteins. {ECO:0000250|UniProtKB:P54307}.
CC -!- SUBUNIT: Homononamer. Interacts with the terminase large subunit gp2;
CC the active complex is probably composed of a one monomer of gp2 and two
CC or more nonamers of gp1. {ECO:0000269|PubMed:22207627}.
CC -!- INTERACTION:
CC P68928; P68928: 1; NbExp=5; IntAct=EBI-15961372, EBI-15961372;
CC -!- SIMILARITY: Belongs to the SPP1-like small terminase family.
CC {ECO:0000305}.
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DR EMBL; X67297; CAA47711.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AM268240; CAK29441.1; -; Genomic_DNA.
DR PDB; 2CMP; X-ray; 1.58 A; A=1-60.
DR PDB; 3ZQM; X-ray; 1.85 A; A/B/C/D/E/F/G/H/I/J=53-120.
DR PDB; 3ZQN; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=53-120.
DR PDB; 3ZQO; X-ray; 1.68 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=53-120.
DR PDB; 3ZQP; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I=1-145.
DR PDB; 3ZQQ; X-ray; 4.00 A; A/B/C=1-145.
DR PDB; 4ZC3; X-ray; 1.40 A; A=1-68.
DR PDBsum; 2CMP; -.
DR PDBsum; 3ZQM; -.
DR PDBsum; 3ZQN; -.
DR PDBsum; 3ZQO; -.
DR PDBsum; 3ZQP; -.
DR PDBsum; 3ZQQ; -.
DR PDBsum; 4ZC3; -.
DR SMR; P68928; -.
DR DIP; DIP-60005N; -.
DR EvolutionaryTrace; P68928; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR Gene3D; 1.10.10.1400; -; 1.
DR InterPro; IPR038713; Terminase_Gp1_N_sf.
DR InterPro; IPR005335; Terminase_ssu.
DR Pfam; PF03592; Terminase_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..145
FT /note="Terminase small subunit"
FT /id="PRO_0000077790"
FT DNA_BIND 1..53
FT /evidence="ECO:0000269|PubMed:22207627,
FT ECO:0000269|PubMed:23545641"
FT REGION 53..120
FT /note="Oligomerization"
FT /evidence="ECO:0000269|PubMed:22207627"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:4ZC3"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:4ZC3"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:4ZC3"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4ZC3"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:4ZC3"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:4ZC3"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3ZQN"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3ZQO"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:3ZQO"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:3ZQO"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:3ZQO"
FT STRAND 125..139
FT /evidence="ECO:0007829|PDB:3ZQP"
SQ SEQUENCE 145 AA; 16010 MW; 85C811F726AAEE59 CRC64;
MKEPKLSPKQ ERFIEEYFIN DMNATKAAIA AGYSKNSASA IGAENLQKPA IRARIDARLK
EINEKKILQA NEVLEHLTRI ALGQEKEQVL MGIGKGAETK THVEVSAKDR IKALELLGKA
HAVFTDKQKV ETNQVIIVDD SGDAE
