TERS_LAMBD
ID TERS_LAMBD Reviewed; 181 AA.
AC P03707;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Terminase small subunit;
DE EC=3.6.4.- {ECO:0000269|PubMed:8611586, ECO:0000303|PubMed:2965248};
DE AltName: Full=DNA-packaging protein Nu1;
DE AltName: Full=Gene product Nu1;
DE Short=gpNu1;
GN Name=Nu1; OrderedLocusNames=lambdap01;
OS Escherichia phage lambda (Bacteriophage lambda).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage lambda DNA.";
RL J. Mol. Biol. 162:729-773(1982).
RN [2]
RP PROTEIN SEQUENCE OF 1-29, FUNCTION, AND DOMAIN.
RX PubMed=9705918; DOI=10.1006/viro.1998.9221;
RA Babbar B.K., Gold M.;
RT "ATP-reactive sites in the bacteriophage lambda packaging protein terminase
RT lie in the N-termini of its subunits, gpA and gpNu1.";
RL Virology 247:251-264(1998).
RN [3]
RP FUNCTION, AND DOMAIN.
RX PubMed=2989542; DOI=10.1016/0022-2836(85)90215-3;
RA Frackman S., Siegele D.A., Feiss M.;
RT "The terminase of bacteriophage lambda. Functional domains for cosB binding
RT and multimer assembly.";
RL J. Mol. Biol. 183:225-238(1985).
RN [4]
RP DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=2965248; DOI=10.1016/0022-2836(88)90391-9;
RA Becker A., Gold M.;
RT "Prediction of an ATP reactive center in the small subunit, gpNu1, of the
RT phage lambda terminase enzyme.";
RL J. Mol. Biol. 199:219-222(1988).
RN [5]
RP DOMAIN, AND INTERACTION WITH THE LARGE TERMINASE SUBUNIT.
RX PubMed=2969839; DOI=10.1093/genetics/119.3.477;
RA Wu W.-F., Christiansen S., Feiss M.;
RT "Domains for protein-protein interactions at the N and C termini of the
RT large subunit of bacteriophage lambda terminase.";
RL Genetics 119:477-484(1988).
RN [6]
RP DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-35, AND CATALYTIC
RP ACTIVITY.
RX PubMed=8611586; DOI=10.1021/bi952322z;
RA Hwang Y., Catalano C.E., Feiss M.;
RT "Kinetic and mutational dissection of the two ATPase activities of
RT terminase, the DNA packaging enzyme of bacteriophage lambda.";
RL Biochemistry 35:2796-2803(1996).
RN [7]
RP DOMAIN.
RX PubMed=10571997; DOI=10.1021/bi991408f;
RA Yang Q., Berton N., Manning M.C., Catalano C.E.;
RT "Domain structure of gpNu1, a phage lambda DNA packaging protein.";
RL Biochemistry 38:14238-14247(1999).
RN [8]
RP SUBUNIT, AND FUNCTION.
RX PubMed=15755448; DOI=10.1016/j.jmb.2005.01.016;
RA Maluf N.K., Yang Q., Catalano C.E.;
RT "Self-association properties of the bacteriophage lambda terminase
RT holoenzyme: implications for the DNA packaging motor.";
RL J. Mol. Biol. 347:523-542(2005).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16618107; DOI=10.1021/bi052284b;
RA Ortega M.E., Catalano C.E.;
RT "Bacteriophage lambda gpNu1 and Escherichia coli IHF proteins cooperatively
RT bind and bend viral DNA: implications for the assembly of a genome-
RT packaging motor.";
RL Biochemistry 45:5180-5189(2006).
RN [10]
RP DOMAIN.
RX PubMed=16008350; DOI=10.1021/bi050333e;
RA Gaussier H., Ortega M.E., Maluf N.K., Catalano C.E.;
RT "Nucleotides regulate the conformational state of the small terminase
RT subunit from bacteriophage lambda: implications for the assembly of a viral
RT genome-packaging motor.";
RL Biochemistry 44:9645-9656(2005).
RN [11]
RP SUBUNIT.
RX PubMed=30541105; DOI=10.1093/nar/gky1217;
RA Ortiz D., delToro D., Ordyan M., Pajak J., Sippy J., Catala A., Oh C.S.,
RA Vu A., Arya G., Feiss M., Smith D.E., Catalano C.E.;
RT "Evidence that a catalytic glutamate and an 'Arginine Toggle' act in
RT concert to mediate ATP hydrolysis and mechanochemical coupling in a viral
RT DNA packaging motor.";
RL Nucleic Acids Res. 47:1404-1415(2019).
RN [12]
RP STRUCTURE BY NMR OF 1-68, DOMAIN, AND DNA-BINDING.
RX PubMed=12049735; DOI=10.1016/s1097-2765(02)00537-3;
RA de Beer T., Fang J., Ortega M., Yang Q., Maes L., Duffy C., Berton N.,
RA Sippy J., Overduin M., Feiss M., Catalano C.E.;
RT "Insights into specific DNA recognition during the assembly of a viral
RT genome packaging machine.";
RL Mol. Cell 9:981-991(2002).
CC -!- FUNCTION: The small subunit is responsible for the binding to multiple
CC recognition elements within the packaging initiation site cos
CC (PubMed:15755448, PubMed:16618107, PubMed:2989542). The terminase lies
CC at a unique vertex of the procapsid and is composed of two subunits, a
CC small terminase subunit involved in viral DNA recognition (binding to
CC packaging sequence cos), and a large terminase subunit possessing
CC endonucleolytic, ATPase and helicase activities (DNA maturation and
CC packaging) (Probable). The terminase binds, cooperatively with the host
CC factor IHFA/IHFB, to the cos site at the junction of adjacent viral
CC genomes in the concatemeric DNA (PubMed:16618107). The endonuclease and
CC helicase activities of the large subunit cleave the viral DNA
CC generating 5'overhangs of 12 bp in length (Probable). The terminase
CC remains bound to the left end of the genome to be packaged, forming a
CC stable DNA-terminase complex (Probable). In a reaction facilitated by
CC the viral assembly catalyst gpFI, the DNA-terminase complex binds to
CC the portal of the procapsid and the terminase packages the viral DNA
CC into the procapsid until the next cos site on the concatemer reaches
CC the complex (Probable). The downstream cos site is then cut generating
CC the mature right end of the genome, the heterotrimer undocks from the
CC DNA-filled head and remains bound to the left end of concatemer's next
CC genome (Probable). {ECO:0000269|PubMed:15755448,
CC ECO:0000269|PubMed:16618107, ECO:0000269|PubMed:2989542, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:2965248, ECO:0000269|PubMed:8611586};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=469 uM for ATP {ECO:0000269|PubMed:8611586};
CC -!- SUBUNIT: Heterotrimer of two small and one large terminase subunits
CC (PubMed:15755448). The catalytically competent terminase is composed of
CC a tetramer of heterotrimers (PubMed:30541105, PubMed:16618107). The
CC tetramer forms a ring structure large enough to encircle duplex DNA
CC (PubMed:30541105). Host IHFA/IHFB induces bending of viral DNA to
CC facilitate the assembly of the terminase tetramer of heterotrimers
CC (PubMed:16618107). Interacts (via C-terminus) with the terminase large
CC subunit (via N-terminus) (PubMed:2969839).
CC {ECO:0000269|PubMed:15755448, ECO:0000269|PubMed:16618107,
CC ECO:0000269|PubMed:2969839, ECO:0000269|PubMed:30541105}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Note=The terminase
CC lies at a unique vertex of the procapsid during viral DNA packaging.
CC {ECO:0000305}.
CC -!- DOMAIN: The N-terminus contains a winged helix-turn-helix (wHTH) that
CC binds the viral DNA (PubMed:12049735) (Probable). The N-terminus also
CC contains an ATPase site that regulates DNA binding activity
CC (PubMed:9705918, PubMed:2965248, PubMed:16008350). The central part
CC contains a region for the self-interaction (PubMed:10571997). the C-
CC terminus contains region of interaction with the terminase large
CC subunit (PubMed:10571997) (Probable). {ECO:0000269|PubMed:10571997,
CC ECO:0000269|PubMed:12049735, ECO:0000269|PubMed:16008350,
CC ECO:0000269|PubMed:2965248, ECO:0000269|PubMed:9705918,
CC ECO:0000305|PubMed:2989542}.
CC -!- SIMILARITY: Belongs to the terminase small subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02459; AAA96533.1; -; Genomic_DNA.
DR PIR; C04333; JVBPNL.
DR RefSeq; NP_040580.1; NC_001416.1.
DR PDB; 1J9I; NMR; -; A/B=1-68.
DR PDB; 6HN7; X-ray; 3.00 A; B=1-98.
DR PDB; 7LW0; X-ray; 2.32 A; A/B/C/D/E/F/G/H=1-56.
DR PDBsum; 1J9I; -.
DR PDBsum; 6HN7; -.
DR PDBsum; 7LW0; -.
DR BMRB; P03707; -.
DR SMR; P03707; -.
DR IntAct; P03707; 6.
DR GeneID; 2703523; -.
DR KEGG; vg:2703523; -.
DR EvolutionaryTrace; P03707; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097710; C:viral terminase, small subunit; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0044374; F:sequence-specific DNA binding, bending; IDA:UniProtKB.
DR GO; GO:0019073; P:viral DNA genome packaging; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR010906; Phage_lambda_Nu1_terminase-ssu.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF07471; Phage_Nu1; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Direct protein sequencing;
KW DNA-binding; Host cytoplasm; Hydrolase; Nucleotide-binding;
KW Reference proteome; Viral genome packaging; Viral release from host cell.
FT CHAIN 1..181
FT /note="Terminase small subunit"
FT /id="PRO_0000077675"
FT REGION 1..29
FT /note="Winged helix-turn-helix (wHTH)"
FT /evidence="ECO:0000269|PubMed:12049735,
FT ECO:0000269|PubMed:16008350"
FT REGION 110..140
FT /note="Self-assembly"
FT /evidence="ECO:0000269|PubMed:10571997"
FT REGION 141..180
FT /note="Binding to terminase large subunit"
FT /evidence="ECO:0000269|PubMed:10571997"
FT COILED 50..109
FT /evidence="ECO:0000255"
FT BINDING 31..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:2965248,
FT ECO:0000305|PubMed:9705918"
FT MUTAGEN 35
FT /note="K->A,D: Decreased ATPase activity."
FT /evidence="ECO:0000269|PubMed:8611586"
FT MUTAGEN 35
FT /note="K->R: No effect on ATPase activity."
FT /evidence="ECO:0000269|PubMed:8611586"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1J9I"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:6HN7"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:6HN7"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:6HN7"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6HN7"
FT HELIX 43..66
FT /evidence="ECO:0007829|PDB:6HN7"
SQ SEQUENCE 181 AA; 20441 MW; A25A5EAEF7BF18A4 CRC64;
MEVNKKQLAD IFGASIRTIQ NWQEQGMPVL RGGGKGNEVL YDSAAVIKWY AERDAEIENE
KLRREVEELR QASEADLQPG TIEYERHRLT RAQADAQELK NARDSAEVVE TAFCTFVLSR
IAGEIASILD GLPLSVQRRF PELENRHVDF LKRDIIKAMN KAAALDELIP GLLSEYIEQS
G
