TERL_BPT4
ID TERL_BPT4 Reviewed; 610 AA.
AC P17312; Q9T0U4; Q9T0U5; Q9T0U6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04146};
DE AltName: Full=DNA-packaging protein {ECO:0000255|HAMAP-Rule:MF_04146};
DE AltName: Full=Gene product 17;
DE Short=gp17;
DE Includes:
DE RecName: Full=ATPase {ECO:0000255|HAMAP-Rule:MF_04146};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04146, ECO:0000269|PubMed:10967092, ECO:0000269|PubMed:12466275, ECO:0000269|PubMed:16987527, ECO:0000269|PubMed:9533879};
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04146};
DE EC=3.1.21.- {ECO:0000255|HAMAP-Rule:MF_04146, ECO:0000305|PubMed:12466275, ECO:0000305|PubMed:15265872, ECO:0000305|PubMed:16987527, ECO:0000305|PubMed:18627466, ECO:0000305|PubMed:8063105, ECO:0000305|PubMed:9533879};
GN Name=17;
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].
RC STRAIN=D;
RX PubMed=2374730; DOI=10.1093/nar/18.13.4005;
RA Powell D., Franklin J., Arisaka F., Mosig G.;
RT "Bacteriophage T4 DNA packaging genes 16 and 17.";
RL Nucleic Acids Res. 18:4005-4005(1990).
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 FUNCTION, CATALYTIC ACTIVITY, AND DNA-BINDING.
RX PubMed=8063105; DOI=10.1016/0378-1119(94)90834-6;
RA Bhattacharyya S.P., Rao V.B.;
RT "Structural analysis of DNA cleaved in vivo by bacteriophage T4
RT terminase.";
RL Gene 146:67-72(1994).
RN [4]
RP ALTERNATIVE INITIATION.
RX PubMed=8921865; DOI=10.1016/0378-1119(96)00299-5;
RA Franklin J.L., Mosig G.;
RT "Expression of the bacteriophage T4 DNA terminase genes 16 and 17 yields
RT multiple proteins.";
RL Gene 177:179-189(1996).
RN [5]
RP FUNCTION, DNA-BINDING, AND CATALYTIC ACTIVITY.
RX PubMed=9533879; DOI=10.1006/jmbi.1998.1619;
RA Franklin J.L., Haseltine D., Davenport L., Mosig G.;
RT "The largest (70 kDa) product of the bacteriophage T4 DNA terminase gene 17
RT binds to single-stranded DNA segments and digests them towards junctions
RT with double-stranded DNA.";
RL J. Mol. Biol. 277:541-557(1998).
RN [6]
RP INTERACTION WITH THE PORTAL PROTEIN.
RX PubMed=10366503; DOI=10.1006/jmbi.1999.2781;
RA Lin H., Rao V.B., Black L.W.;
RT "Analysis of capsid portal protein and terminase functional domains:
RT interaction sites required for DNA packaging in bacteriophage T4.";
RL J. Mol. Biol. 289:249-260(1999).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION, ACTIVITY
RP REGULATION, AND PHOSPHORYLATION.
RX PubMed=10967092; DOI=10.1074/jbc.m003357200;
RA Leffers G., Rao V.B.;
RT "Biochemical characterization of an ATPase activity associated with the
RT large packaging subunit gp17 from bacteriophage T4.";
RL J. Biol. Chem. 275:37127-37136(2000).
RN [8]
RP DOMAIN, FUNCTION, AND MUTAGENESIS OF GLY-165; LYS-166 AND THR-167.
RX PubMed=11846554; DOI=10.1006/jmbi.2001.5169;
RA Rao V.B., Mitchell M.S.;
RT "The N-terminal ATPase site in the large terminase protein gp17 is
RT critically required for DNA packaging in bacteriophage T4.";
RL J. Mol. Biol. 314:401-411(2001).
RN [9]
RP DOMAIN.
RX PubMed=12235385; DOI=10.1093/nar/gkf524;
RA Mitchell M.S., Matsuzaki S., Imai S., Rao V.B.;
RT "Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and
RT 17 reveals a common ATPase center in the large subunit of viral
RT terminases.";
RL Nucleic Acids Res. 30:4009-4021(2002).
RN [10]
RP INTERACTION WITH GP55.
RX PubMed=12051907; DOI=10.1016/s0022-2836(02)00298-x;
RA Malys N., Chang D.Y., Baumann R.G., Xie D., Black L.W.;
RT "A bipartite bacteriophage T4 SOC and HOC randomized peptide display
RT library: detection and analysis of phage T4 terminase (gp17) and late sigma
RT factor (gp55) interaction.";
RL J. Mol. Biol. 319:289-304(2002).
RN [11]
RP INTERACTION WITH THE TERMINASE SMALL SUBUNIT, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=12466275; DOI=10.1074/jbc.m208574200;
RA Baumann R.G., Black L.W.;
RT "Isolation and characterization of T4 bacteriophage gp17 terminase, a large
RT subunit multimer with enhanced ATPase activity.";
RL J. Biol. Chem. 278:4618-4627(2003).
RN [12]
RP MUTAGENESIS OF GLU-256, AND ACTIVE SITE.
RX PubMed=12875841; DOI=10.1016/s0022-2836(03)00636-3;
RA Goetzinger K.R., Rao V.B.;
RT "Defining the ATPase center of bacteriophage T4 DNA packaging machine:
RT requirement for a catalytic glutamate residue in the large terminase
RT protein gp17.";
RL J. Mol. Biol. 331:139-154(2003).
RN [13]
RP CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=15265872; DOI=10.1074/jbc.m403647200;
RA Kanamaru S., Kondabagil K., Rossmann M.G., Rao V.B.;
RT "The functional domains of bacteriophage t4 terminase.";
RL J. Biol. Chem. 279:40795-40801(2004).
RN [14]
RP MUTAGENESIS OF TYR-253 AND ASP-255.
RX PubMed=16258174; DOI=10.1074/jbc.m507719200;
RA Mitchell M.S., Rao V.B.;
RT "Functional analysis of the bacteriophage T4 DNA-packaging ATPase motor.";
RL J. Biol. Chem. 281:518-527(2006).
RN [15]
RP DOMAIN, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP LYS-166; ASP-255 AND GLU-256.
RX PubMed=16987527; DOI=10.1016/j.jmb.2006.08.054;
RA Kondabagil K.R., Zhang Z., Rao V.B.;
RT "The DNA translocating ATPase of bacteriophage T4 packaging motor.";
RL J. Mol. Biol. 363:786-799(2006).
RN [16]
RP CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, AND MUTAGENESIS OF ASP-401;
RP GLU-404; GLY-405; ASP-409; GLU-458 AND ASP-542.
RX PubMed=18627466; DOI=10.1111/j.1365-2958.2008.06344.x;
RA Alam T.I., Draper B., Kondabagil K., Rentas F.J., Ghosh-Kumar M., Sun S.,
RA Rossmann M.G., Rao V.B.;
RT "The headful packaging nuclease of bacteriophage T4.";
RL Mol. Microbiol. 69:1180-1190(2008).
RN [17]
RP REVIEW.
RX PubMed=18687036; DOI=10.1146/annurev.genet.42.110807.091545;
RA Rao V.B., Feiss M.;
RT "The bacteriophage DNA packaging motor.";
RL Annu. Rev. Genet. 42:647-681(2008).
RN [18]
RP DNA-BINDING, AND DOMAIN.
RX PubMed=18234214; DOI=10.1016/j.jmb.2007.12.041;
RA Alam T.I., Rao V.B.;
RT "The ATPase domain of the large terminase protein, gp17, from bacteriophage
RT T4 binds DNA: implications to the DNA packaging mechanism.";
RL J. Mol. Biol. 376:1272-1281(2008).
RN [19]
RP INTERACTION WITH THE PORTAL PROTEIN, AND DOMAIN.
RX PubMed=22345478; DOI=10.1128/jvi.07197-11;
RA Hegde S., Padilla-Sanchez V., Draper B., Rao V.B.;
RT "Portal-large terminase interactions of the bacteriophage T4 DNA packaging
RT machine implicate a molecular lever mechanism for coupling ATPase to DNA
RT translocation.";
RL J. Virol. 86:4046-4057(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 1-360, ACTIVE SITE, MUTAGENESIS
RP OF ASP-255 AND GLU-256, AND COFACTOR.
RX PubMed=17386269; DOI=10.1016/j.molcel.2007.02.013;
RA Sun S., Kondabagil K., Gentz P.M., Rossmann M.G., Rao V.B.;
RT "The structure of the ATPase that powers DNA packaging into bacteriophage
RT T4 procapsids.";
RL Mol. Cell 25:943-949(2007).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-567, AND COFACTOR.
RX PubMed=19109896; DOI=10.1016/j.cell.2008.11.015;
RA Sun S., Kondabagil K., Draper B., Alam T.I., Bowman V.D., Zhang Z.,
RA Hegde S., Fokine A., Rossmann M.G., Rao V.B.;
RT "The structure of the phage T4 DNA packaging motor suggests a mechanism
RT dependent on electrostatic forces.";
RL Cell 135:1251-1262(2008).
CC -!- FUNCTION: [Isoform Terminase large subunit]: The terminase large
CC subunit acts as an ATP driven molecular motor necessary for viral DNA
CC translocation into empty capsids and as an endonuclease that cuts the
CC viral genome to initiate and to end a packaging reaction
CC (PubMed:11846554, PubMed:10967092, PubMed:12466275). 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 (packaging
CC sequence), and a large terminase subunit possessing endonucleolytic and
CC ATPase activities (PubMed:12466275). Both terminase subunits
CC heterooligomerize and are docked on the portal protein to form the
CC packaging machine. The terminase large subunit exhibits endonuclease
CC activity and cleaves the viral genome concatemer once the capsid is
CC full (headful packaging) (PubMed:8063105, PubMed:10967092,
CC PubMed:12466275). Once the capsid is packaged with the DNA, the
CC terminase complex is substituted by the tail. {ECO:0000255|HAMAP-
CC Rule:MF_04146, ECO:0000269|PubMed:10967092,
CC ECO:0000269|PubMed:11846554, ECO:0000269|PubMed:12466275,
CC ECO:0000269|PubMed:8063105}.
CC -!- COFACTOR: [Isoform Terminase large subunit]:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04146,
CC ECO:0000269|PubMed:18627466, ECO:0000305|PubMed:19109896};
CC Note=ATPase activity requires 1 Mg(2+) ion per subunit
CC (PubMed:17386269). Nuclease activity probably requires 2 Mg(2+) ions
CC per subunit (PubMed:19109896). {ECO:0000255|HAMAP-Rule:MF_04146,
CC ECO:0000269|PubMed:17386269, ECO:0000269|PubMed:19109896};
CC -!- ACTIVITY REGULATION: [Isoform Terminase large subunit]: Stimulated up
CC to 50 to 100-fold by the terminase small subunit (By similarity)
CC (PubMed:10967092, PubMed:12466275, PubMed:16987527). Modestly activated
CC by portal protein and single-stranded binding protein gp32 multimers
CC (PubMed:12466275). {ECO:0000255|HAMAP-Rule:MF_04146,
CC ECO:0000269|PubMed:10967092, ECO:0000269|PubMed:12466275,
CC ECO:0000269|PubMed:16987527}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform Terminase large subunit]:
CC Kinetic parameters:
CC KM=380 uM for ATP {ECO:0000269|PubMed:12466275};
CC KM=256 uM for ATP {ECO:0000269|PubMed:10967092};
CC Note=The Km values for the ATPase activity were measured in presence
CC of gp16. {ECO:0000269|PubMed:10967092, ECO:0000269|PubMed:12466275};
CC -!- SUBUNIT: [Isoform Terminase large subunit]: Interacts with the
CC terminase small subunit; the active complex is composed of a pentamer
CC of terminase large subunits and a dodecamer of terminase small subunits
CC (PubMed:12466275, PubMed:17386269). Interacts with the portal protein
CC (PubMed:10366503, PubMed:22345478). Interacts with the RNA polymerase
CC sigma factor gp55 (By similarity) (PubMed:12051907).
CC {ECO:0000255|HAMAP-Rule:MF_04146, ECO:0000269|PubMed:10366503,
CC ECO:0000269|PubMed:12051907, ECO:0000269|PubMed:12466275,
CC ECO:0000269|PubMed:17386269, ECO:0000269|PubMed:22345478}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=4;
CC Comment=Several shorter peptides are initiated at internal ribosome
CC binding sites and translated in the same reading frame as gp17.
CC {ECO:0000269|PubMed:8921865};
CC Name=Terminase large subunit;
CC IsoId=P17312-1; Sequence=Displayed;
CC Name=Gp17'A;
CC IsoId=P17312-2; Sequence=VSP_018679;
CC Name=Gp17'B;
CC IsoId=P17312-3; Sequence=VSP_018680;
CC Name=Gp17'';
CC IsoId=P17312-4; Sequence=VSP_018681;
CC -!- DOMAIN: [Isoform Terminase large subunit]: The N-terminus contains an
CC ATPase domain (PubMed:12235385, PubMed:11846554, PubMed:16987527,
CC PubMed:15265872). The ATPase domain binds to dsDNA in a sequence non-
CC specific manner (PubMed:18234214). The C-terminus contains an
CC endonuclease domain (PubMed:12235385, PubMed:16987527,
CC PubMed:15265872). The terminase nuclease domain binds ssDNA but not
CC dsDNA (PubMed:8063105, PubMed:9533879). {ECO:0000269|PubMed:11846554,
CC ECO:0000269|PubMed:12235385, ECO:0000269|PubMed:15265872,
CC ECO:0000269|PubMed:16987527, ECO:0000269|PubMed:18234214,
CC ECO:0000269|PubMed:8063105, ECO:0000269|PubMed:9533879}.
CC -!- PTM: [Isoform Terminase large subunit]: Phosphorylated.
CC {ECO:0000269|PubMed:10967092}.
CC -!- SIMILARITY: Belongs to the Tequatrovirus large terminase family.
CC {ECO:0000255|HAMAP-Rule:MF_04146}.
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DR EMBL; X52394; CAA36641.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42422.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42684.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42685.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42686.1; -; Genomic_DNA.
DR PIR; JU0287; GVBPT4.
DR RefSeq; NP_049776.1; NC_000866.4. [P17312-1]
DR RefSeq; NP_049777.1; NC_000866.4. [P17312-2]
DR RefSeq; NP_049778.1; NC_000866.4. [P17312-3]
DR RefSeq; NP_049779.1; NC_000866.4. [P17312-4]
DR PDB; 2O0H; X-ray; 1.88 A; A=1-360.
DR PDB; 2O0J; X-ray; 1.80 A; A=1-360.
DR PDB; 2O0K; X-ray; 2.50 A; A=1-360.
DR PDB; 3CPE; X-ray; 2.80 A; A=1-567.
DR PDB; 3EZK; EM; 34.00 A; A/B/C/D/E=1-577.
DR PDBsum; 2O0H; -.
DR PDBsum; 2O0J; -.
DR PDBsum; 2O0K; -.
DR PDBsum; 3CPE; -.
DR PDBsum; 3EZK; -.
DR SMR; P17312; -.
DR DIP; DIP-60322N; -.
DR IntAct; P17312; 1.
DR GeneID; 1258545; -.
DR GeneID; 1258647; -.
DR GeneID; 1258656; -.
DR GeneID; 1258675; -.
DR KEGG; vg:1258545; -.
DR KEGG; vg:1258647; -.
DR KEGG; vg:1258656; -.
DR KEGG; vg:1258675; -.
DR EvolutionaryTrace; P17312; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098009; C:viral terminase, large subunit; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:CACAO.
DR GO; GO:0004536; F:deoxyribonuclease activity; IMP:CACAO.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004518; F:nuclease activity; IDA:UniProtKB.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR GO; GO:0019072; P:viral genome packaging; IDA:UniProtKB.
DR GO; GO:0046797; P:viral procapsid maturation; IDA:CACAO.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04146; TERL_T4; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035421; Terminase_6C.
DR InterPro; IPR044267; Terminase_large_su_gp17-like.
DR Pfam; PF17289; Terminase_6C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; ATP-binding; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Nucleotide-binding; Reference proteome;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..610
FT /note="Terminase, large subunit"
FT /id="PRO_0000003331"
FT REGION 30..94
FT /note="ssDNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:9533879"
FT REGION 131..301
FT /note="ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:12235385"
FT REGION 328..352
FT /note="Binding to the portal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:22345478"
FT REGION 360..559
FT /note="Nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:12235385"
FT MOTIF 161..167
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:11846554, ECO:0000269|PubMed:12235385"
FT MOTIF 251..256
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:12235385"
FT MOTIF 285..287
FT /note="ATPase coupling"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:12235385"
FT ACT_SITE 256
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:12875841, ECO:0000269|PubMed:17386269"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:17386269"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:17386269"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:17386269"
FT BINDING 401
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000305|PubMed:18627466, ECO:0000305|PubMed:19109896"
FT BINDING 401
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000305|PubMed:18627466, ECO:0000305|PubMed:19109896"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000305|PubMed:18627466, ECO:0000305|PubMed:19109896"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000305|PubMed:18627466, ECO:0000305|PubMed:19109896"
FT SITE 409
FT /note="Modulates nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000269|PubMed:18627466"
FT VAR_SEQ 1..194
FT /note="Missing (in isoform Gp17'')"
FT /evidence="ECO:0000305"
FT /id="VSP_018681"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform Gp17'B)"
FT /evidence="ECO:0000305"
FT /id="VSP_018680"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform Gp17'A)"
FT /evidence="ECO:0000305"
FT /id="VSP_018679"
FT MUTAGEN 165
FT /note="G->A: Complete loss of in vitro DNA packaging
FT activity but not the endonuclease activity."
FT /evidence="ECO:0000269|PubMed:11846554"
FT MUTAGEN 166
FT /note="K->G: Complete loss of in vitro DNA packaging
FT activity. No effect on in vivo terminase activity. Loss of
FT terminase small subunit-stimulated ATPase activity."
FT /evidence="ECO:0000269|PubMed:11846554"
FT MUTAGEN 166
FT /note="K->R: Complete loss of in vitro DNA packaging
FT activity but not the endonuclease activity."
FT /evidence="ECO:0000269|PubMed:11846554,
FT ECO:0000269|PubMed:16987527"
FT MUTAGEN 167
FT /note="T->A: Complete loss of in vitro DNA packaging
FT activity but not the endonuclease activity."
FT /evidence="ECO:0000269|PubMed:11846554"
FT MUTAGEN 253
FT /note="Y->A,G,K,P,R: Complete loss of terminase small
FT subunit-stimulated ATPase activity."
FT /evidence="ECO:0000269|PubMed:16258174,
FT ECO:0000269|PubMed:17386269"
FT MUTAGEN 255
FT /note="D->E: Almost complete loss of terminase small
FT subunit-stimulated ATPase activity."
FT /evidence="ECO:0000269|PubMed:16258174,
FT ECO:0000269|PubMed:16987527, ECO:0000269|PubMed:17386269"
FT MUTAGEN 255
FT /note="D->N,T,V: Complete loss of terminase small subunit-
FT stimulated ATPase activity."
FT /evidence="ECO:0000269|PubMed:16258174"
FT MUTAGEN 256
FT /note="E->D: Complete loss of terminase small subunit-
FT stimulated ATPase activity and in vitro DNA packaging
FT activity. No effect on ATP binding and endonuclease
FT functions."
FT /evidence="ECO:0000269|PubMed:12875841,
FT ECO:0000269|PubMed:16987527, ECO:0000269|PubMed:17386269"
FT MUTAGEN 256
FT /note="E->Q: Complete loss of terminase small subunit-
FT stimulated ATPase activity and in vitro DNA packaging
FT activity. No effect on ATP binding and endonuclease
FT functions."
FT /evidence="ECO:0000269|PubMed:12875841"
FT MUTAGEN 256
FT /note="E->V: Complete loss of terminase small subunit-
FT stimulated ATPase activity and in vitro DNA packaging
FT activity. No effect on ATP binding and endonuclease
FT functions."
FT /evidence="ECO:0000269|PubMed:12875841,
FT ECO:0000269|PubMed:17386269"
FT MUTAGEN 401
FT /note="D->N: Complete loss of nuclease activity. Almost no
FT circular DNA packaging."
FT /evidence="ECO:0000269|PubMed:18627466"
FT MUTAGEN 404
FT /note="E->N: Complete loss of nuclease activity. Almost no
FT circular DNA packaging."
FT /evidence="ECO:0000269|PubMed:18627466"
FT MUTAGEN 405
FT /note="G->V: Complete loss of nuclease activity. Almost no
FT circular DNA packaging."
FT /evidence="ECO:0000269|PubMed:18627466"
FT MUTAGEN 409
FT /note="D->N: Enhanced nuclease activity. Normal circular
FT DNA packaging."
FT /evidence="ECO:0000269|PubMed:18627466"
FT MUTAGEN 458
FT /note="E->A: Complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:18627466"
FT MUTAGEN 542
FT /note="D->A: Complete loss of nuclease activity. Unable to
FT package circular plasmid DNA but packages linear DNA."
FT /evidence="ECO:0000269|PubMed:18627466"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2O0K"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2O0K"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2O0J"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2O0H"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 193..209
FT /evidence="ECO:0007829|PDB:2O0J"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:2O0J"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2O0K"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2O0K"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:2O0J"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:2O0J"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:3CPE"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 419..434
FT /evidence="ECO:0007829|PDB:3CPE"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:3CPE"
FT HELIX 439..449
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:3CPE"
FT HELIX 461..471
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:3CPE"
FT HELIX 493..508
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:3CPE"
FT HELIX 517..523
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:3CPE"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:3CPE"
FT HELIX 542..555
FT /evidence="ECO:0007829|PDB:3CPE"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:3CPE"
SQ SEQUENCE 610 AA; 69756 MW; 5BC2F4BEC3EC79E4 CRC64;
MEQPINVLND FHPLNEAGKI LIKHPSLAER KDEDGIHWIK SQWDGKWYPE KFSDYLRLHK
IVKIPNNSDK PELFQTYKDK NNKRSRYMGL PNLKRANIKT QWTREMVEEW KKCRDDIVYF
AETYCAITHI DYGVIKVQLR DYQRDMLKIM SSKRMTVCNL SRQLGKTTVV AIFLAHFVCF
NKDKAVGILA HKGSMSAEVL DRTKQAIELL PDFLQPGIVE WNKGSIELDN GSSIGAYASS
PDAVRGNSFA MIYIDECAFI PNFHDSWLAI QPVISSGRRS KIIITTTPNG LNHFYDIWTA
AVEGKSGFEP YTAIWNSVKE RLYNDEDIFD DGWQWSIQTI NGSSLAQFRQ EHTAAFEGTS
GTLISGMKLA VMDFIEVTPD DHGFHQFKKP EPDRKYIATL DCSEGRGQDY HALHIIDVTD
DVWEQVGVLH SNTISHLILP DIVMRYLVEY NECPVYIELN STGVSVAKSL YMDLEYEGVI
CDSYTDLGMK QTKRTKAVGC STLKDLIEKD KLIIHHRATI QEFRTFSEKG VSWAAEEGYH
DDLVMSLVIF GWLSTQSKFI DYADKDDMRL ASEVFSKELQ DMSDDYAPVI FVDSVHSAEY
VPVSHGMSMV
