TERL_LAMBD
ID TERL_LAMBD Reviewed; 641 AA.
AC P03708;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000303|PubMed:22191393};
DE AltName: Full=DNA-packaging protein A;
DE AltName: Full=Large terminase protein {ECO:0000255|HAMAP-Rule:MF_04144};
DE AltName: Full=gpA;
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04144};
DE EC=3.1.21.4 {ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:1534952, ECO:0000269|PubMed:17870092, ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:2970303, ECO:0000269|PubMed:7813453, ECO:0000269|PubMed:8794874};
DE Includes:
DE RecName: Full=Helicase {ECO:0000255|HAMAP-Rule:MF_04144};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:8175794};
DE Includes:
DE RecName: Full=ATPase {ECO:0000255|HAMAP-Rule:MF_04144};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:10993723, ECO:0000269|PubMed:11866517, ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:30541105, ECO:0000269|PubMed:8428984};
GN Name=A; OrderedLocusNames=lambdap02;
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 59-70, DOMAIN, AND SUBUNIT.
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.
RX PubMed=860405; DOI=10.1016/0042-6822(77)90100-3;
RA Becker A., Marko M., Gold M.;
RT "Early events in the in vitro packaging of bacteriophage lambda DNA.";
RL Virology 78:291-305(1977).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=6315731; DOI=10.1016/s0021-9258(17)43907-x;
RA Gold M., Becker A.;
RT "The bacteriophage lambda terminase. Partial purification and preliminary
RT characterization of properties.";
RL J. Biol. Chem. 258:14619-14625(1983).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2970303; DOI=10.1016/s0092-8674(88)91021-5;
RA Higgins R.R., Lucko H.J., Becker A.;
RT "Mechanism of cos DNA cleavage by bacteriophage lambda terminase: multiple
RT roles of ATP.";
RL Cell 54:765-775(1988).
RN [6]
RP FUNCTION.
RX PubMed=2965251; DOI=10.1016/0022-2836(88)90304-x;
RA Becker A., Murialdo H., Lucko H., Morell J.;
RT "Bacteriophage lambda DNA packaging. The product of the FI gene promotes
RT the incorporation of the prohead to the DNA-terminase complex.";
RL J. Mol. Biol. 199:597-607(1988).
RN [7]
RP DOMAIN, INTERACTION WITH THE SMALL TERMINASE SUBUNIT, AND INTERACTION WITH
RP THE PORTAL PROTEIN.
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 [8]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-401 AND GLU-586, AND DOMAIN.
RX PubMed=1534952; DOI=10.1016/0042-6822(92)90677-h;
RA Davidson A.R., Gold M.;
RT "Mutations abolishing the endonuclease activity of bacteriophage lambda
RT terminase lie in two distinct regions of the A gene, one of which may
RT encode a 'leucine zipper' DNA-binding domain.";
RL Virology 189:21-30(1992).
RN [9]
RP SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8428984; DOI=10.1016/s0021-9258(18)53659-0;
RA Tomka M.A., Catalano C.E.;
RT "Physical and kinetic characterization of the DNA packaging enzyme from
RT bacteriophage lambda.";
RL J. Biol. Chem. 268:3056-3065(1993).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=8175794; DOI=10.1016/s0021-9258(17)36870-9;
RA Rubinchik S., Parris W., Gold M.;
RT "The in vitro ATPases of bacteriophage lambda terminase and its large
RT subunit, gene product A. The relationship with their DNA helicase and
RT packaging activities.";
RL J. Biol. Chem. 269:13586-13593(1994).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7813453; DOI=10.1002/j.1460-2075.1994.tb06963.x;
RA Higgins R.R., Becker A.;
RT "The lambda terminase enzyme measures the point of its endonucleolytic
RT attack 47 +/- 2 bp away from its site of specific DNA binding, the R
RT site.";
RL EMBO J. 13:6162-6171(1994).
RN [12]
RP INTERACTION WITH THE PORTAL PROTEIN.
RX PubMed=7799432; DOI=10.1006/jmbi.1994.0013;
RA Yeo A., Feiss M.;
RT "Specific interaction of terminase, the DNA packaging enzyme of
RT bacteriophage lambda, with the portal protein of the prohead.";
RL J. Mol. Biol. 245:141-150(1995).
RN [13]
RP MUTAGENESIS OF LYS-497, AND DOMAIN.
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 [14]
RP MUTAGENESIS OF LYS-497, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
RP DOMAIN, AND SUBUNIT.
RX PubMed=8794874; DOI=10.1006/jmbi.1996.0480;
RA Hwang Y., Feiss M.;
RT "Mutations affecting the high affinity ATPase center of gpA, the large
RT subunit of bacteriophage lambda terminase, inactivate the endonuclease
RT activity of terminase.";
RL J. Mol. Biol. 261:524-535(1996).
RN [15]
RP DOMAIN, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-46 AND LYS-84, AND SUBUNIT.
RX PubMed=10993723; DOI=10.1006/jmbi.2000.4086;
RA Hang J.Q., Tack B.F., Feiss M.;
RT "ATPase center of bacteriophage lambda terminase involved in post-cleavage
RT stages of DNA packaging: identification of ATP-interactive amino acids.";
RL J. Mol. Biol. 302:777-795(2000).
RN [16]
RP FUNCTION, MUTAGENESIS OF GLY-18; LYS-76; ASN-166; LEU-180; GLY-191;
RP THR-194; GLY-212; ARG-225; THR-328 AND ASP-349, CATALYTIC ACTIVITY, AND
RP DOMAIN.
RX PubMed=11866517; DOI=10.1006/jmbi.2001.5368;
RA Duffy C., Feiss M.;
RT "The large subunit of bacteriophage lambda's terminase plays a role in DNA
RT translocation and packaging termination.";
RL J. Mol. Biol. 316:547-561(2002).
RN [17]
RP SUBUNIT.
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 [18]
RP SUBUNIT.
RX PubMed=17176048; DOI=10.1021/bi0615036;
RA Maluf N.K., Gaussier H., Bogner E., Feiss M., Catalano C.E.;
RT "Assembly of bacteriophage lambda terminase into a viral DNA maturation and
RT packaging machine.";
RL Biochemistry 45:15259-15268(2006).
RN [19]
RP DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=17870092; DOI=10.1016/j.jmb.2007.07.067;
RA Ortega M.E., Gaussier H., Catalano C.E.;
RT "The DNA maturation domain of gpA, the DNA packaging motor protein of
RT bacteriophage lambda, contains an ATPase site associated with endonuclease
RT activity.";
RL J. Mol. Biol. 373:851-865(2007).
RN [20]
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 [21]
RP MUTAGENESIS OF TYR-46; LYS-76 AND LYS-84, AND DOMAIN.
RX PubMed=19706522; DOI=10.1073/pnas.0904364106;
RA Tsay J.M., Sippy J., Feiss M., Smith D.E.;
RT "The Q motif of a viral packaging motor governs its force generation and
RT communicates ATP recognition to DNA interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14355-14360(2009).
RN [22]
RP FUNCTION.
RX PubMed=22191393; DOI=10.1021/bi201604b;
RA Chang J.R., Andrews B.T., Catalano C.E.;
RT "Energy-independent helicase activity of a viral genome packaging motor.";
RL Biochemistry 51:391-400(2012).
RN [23]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23134123; DOI=10.1021/bi300890y;
RA Andrews B.T., Catalano C.E.;
RT "The enzymology of a viral genome packaging motor is influenced by the
RT assembly state of the motor subunits.";
RL Biochemistry 51:9342-9353(2012).
RN [24]
RP MUTAGENESIS OF LYS-76.
RX PubMed=23530228; DOI=10.1073/pnas.1222820110;
RA Andrews B.T., Catalano C.E.;
RT "Strong subunit coordination drives a powerful viral DNA packaging motor.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5909-5914(2013).
RN [25]
RP MUTAGENESIS OF LYS-76; SER-77; ALA-78; ARG-79; VAL-80; GLY-81; TYR-82;
RP SER-83 AND LYS-84.
RX PubMed=27139643; DOI=10.1016/j.jmb.2016.04.029;
RA delToro D., Ortiz D., Ordyan M., Sippy J., Oh C.S., Keller N., Feiss M.,
RA Catalano C.E., Smith D.E.;
RT "Walker-A motif acts to coordinate ATP hydrolysis with motor output in
RT viral DNA packaging.";
RL J. Mol. Biol. 428:2709-2729(2016).
RN [26]
RP FUNCTION, AND SUBUNIT.
RX PubMed=28445747; DOI=10.1016/j.bpj.2017.02.041;
RA Yang T.C., Ortiz D., Yang Q., De Angelis R.W., Sanyal S.J., Catalano C.E.;
RT "Physical and functional characterization of a viral genome maturation
RT complex.";
RL Biophys. J. 112:1551-1560(2017).
RN [27]
RP SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLU-179, CATALYTIC ACTIVITY, AND
RP REACTION MECHANISM.
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).
CC -!- FUNCTION: The terminase large subunit acts as an ATP driven molecular
CC motor necessary for viral DNA translocation into empty capsids and as
CC an endonuclease that cuts the viral genome from the concetamer to
CC initiate and to end the packaging reaction (PubMed:11866517,
CC PubMed:23134123). The terminase lies at a unique vertex of the
CC procapsid and is composed of two subunits, a small terminase subunit
CC involved in viral DNA recognition (binding to packaging sequence cos),
CC and a large terminase subunit possessing endonucleolytic, ATPase and
CC helicase activities (DNA maturation and packaging) (PubMed:11866517,
CC PubMed:23134123). The terminase binds cooperatively with the host
CC factor IHFA/IHFB to the cos site at the junction of adjacent viral
CC genomes (PubMed:22191393, PubMed:15755448, PubMed:28445747). The
CC endonuclease activity cleaves the viral DNA generating 5'overhangs of
CC 12 bp in length (PubMed:6315731, PubMed:2970303, PubMed:8428984,
CC PubMed:7813453). The helicase activity separates the cohesive ends
CC generating the single-stranded 'sticky' ends of the mature genome
CC (PubMed:6315731, PubMed:2970303, PubMed:8175794). IHFA/IHFB is also
CC necessary for the strand separation activity of the terminase
CC (PubMed:22191393). The terminase remains bound to the left end of the
CC genome to be packaged, forming a stable DNA-terminase complex
CC (PubMed:860405). In a reaction facilitated by the viral assembly
CC catalyst gpFI, the DNA-terminase complex binds to the portal of the
CC procapsid thereby activating the translocase activity of the terminase
CC (PubMed:2965251). The terminase packages the viral DNA into the
CC procapsid until the next cos site on the concatemer reaches the complex
CC (PubMed:860405, PubMed:2965251) (Probable). The downstream cos site is
CC then cut generating the mature right end of the genome, the
CC heterotrimer undocks from the DNA-filled head and remains bound to the
CC left end of concatemer's next genome (PubMed:2970303).
CC {ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:11866517,
CC ECO:0000269|PubMed:15755448, ECO:0000269|PubMed:22191393,
CC ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:28445747,
CC ECO:0000269|PubMed:2965251, ECO:0000269|PubMed:2970303,
CC ECO:0000269|PubMed:6315731, ECO:0000269|PubMed:7813453,
CC ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984,
CC ECO:0000269|PubMed:860405, ECO:0000305|PubMed:11866517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04144,
CC ECO:0000269|PubMed:1534952, ECO:0000269|PubMed:17870092,
CC ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:2970303,
CC ECO:0000269|PubMed:7813453};
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; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04144,
CC ECO:0000269|PubMed:10993723, ECO:0000269|PubMed:11866517,
CC ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:30541105,
CC ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984,
CC ECO:0000269|PubMed:8794874};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04144,
CC ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984};
CC Note=Probably binds 2 Mg(2+) ions per subunit (By similarity).
CC Necessary for the ATPase activity (PubMed:8428984, PubMed:8175794).
CC Zn(2+) Co(2+), Cd(2+), Cu(2+), Ca(2+), Sr(2+) and Ba(2+) do not
CC function as cofactor (PubMed:8428984). {ECO:0000250|UniProtKB:P0A7Y4,
CC ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984};
CC -!- ACTIVITY REGULATION: Inhibited by NaCl and KC1 at concentrations higher
CC than 100 mM and by glutamate at concentrations greater than 150 mM.
CC {ECO:0000269|PubMed:8428984}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 uM for ATP for the high affinity ATPase
CC {ECO:0000269|PubMed:8428984, ECO:0000269|PubMed:8611586,
CC ECO:0000269|PubMed:8794874};
CC KM=23 uM for ATP for helicase {ECO:0000269|PubMed:8175794};
CC Note=The high affinity ATPase activity corresponds to the packaging
CC ATPase site at the N-terminus. {ECO:0000269|PubMed:11866517,
CC ECO:0000303|PubMed:17870092};
CC pH dependence:
CC Optimum pH is 8.0-9.0 for the ATPase and helicase.
CC {ECO:0000269|PubMed:8175794};
CC -!- SUBUNIT: Heterotrimer of two small and one large terminase subunits
CC (Probable) (PubMed:6315731, PubMed:15755448, PubMed:8428984,
CC PubMed:30541105). The catalytically competent terminase is composed of
CC a tetramer of heterotrimers (PubMed:30541105, PubMed:28445747,
CC PubMed:8175794, PubMed:8794874, PubMed:9705918, PubMed:10993723). 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:17176048, PubMed:28445747). Interacts (via N-terminus) with the
CC terminase small subunit (via C-terminus) (PubMed:2969839). Interacts
CC (via C-terminus) with the portal protein; this interaction allows the
CC packaging of viral DNA (PubMed:7799432). {ECO:0000255|HAMAP-
CC Rule:MF_04144, ECO:0000269|PubMed:10993723,
CC ECO:0000269|PubMed:15755448, ECO:0000269|PubMed:17176048,
CC ECO:0000269|PubMed:28445747, ECO:0000269|PubMed:2969839,
CC ECO:0000269|PubMed:30541105, ECO:0000269|PubMed:6315731,
CC ECO:0000269|PubMed:7799432, ECO:0000269|PubMed:8175794,
CC ECO:0000269|PubMed:8428984, ECO:0000269|PubMed:8794874,
CC ECO:0000269|PubMed:9705918, ECO:0000305|PubMed:2969839}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04144}.
CC Note=The terminase lies at a unique vertex of the procapsid during
CC viral DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04144}.
CC -!- DOMAIN: The N-terminus is involved in the formation of the heterotrimer
CC with the small subunit (PubMed:2969839). The N-terminus part contains
CC the translocase activity involved in DNA packaging (PubMed:11866517).
CC At the N-terminus, there is a high affinity ATPase center that is
CC probably needed for the packaging activity (PubMed:8611586,
CC PubMed:8794874, PubMed:19706522, PubMed:9705918, PubMed:10993723). The
CC Walker A motif of the ATPase center is responsible for interacting with
CC the ATP phosphate and the Q motif governs force generation and the
CC interaction with DNA (PubMed:19706522). The C-terminus contains the
CC site specific endonuclease (cos-cleavage) and strand separation
CC (helicase) activities required for genome maturation (PubMed:17870092).
CC A second ATPase catalytic site regulates the genome maturation
CC (PubMed:17870092). The C-terminus very end is involved in binding to
CC the procapsid (PubMed:2969839). Contains a basic leucine zipper (bZIP)
CC that may be involved in the formation of the terminase (PubMed:1534952)
CC (Probable). {ECO:0000255|HAMAP-Rule:MF_04144,
CC ECO:0000269|PubMed:10993723, ECO:0000269|PubMed:11866517,
CC ECO:0000269|PubMed:1534952, ECO:0000269|PubMed:17870092,
CC ECO:0000269|PubMed:19706522, ECO:0000269|PubMed:2969839,
CC ECO:0000269|PubMed:8611586, ECO:0000269|PubMed:8794874,
CC ECO:0000269|PubMed:9705918, ECO:0000305|PubMed:17176048}.
CC -!- SIMILARITY: Belongs to the lambdavirus large terminase family.
CC {ECO:0000255|HAMAP-Rule:MF_04144}.
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DR EMBL; J02459; AAA96534.1; -; Genomic_DNA.
DR PIR; D04333; JVBPAL.
DR RefSeq; NP_040581.1; NC_001416.1.
DR IntAct; P03708; 10.
DR GeneID; 2703524; -.
DR KEGG; vg:2703524; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098009; C:viral terminase, large subunit; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04144; TERL_LAMBDA; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008866; Phage_lambda_GpA-like.
DR Pfam; PF05876; Terminase_GpA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Endonuclease; Host cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome; Viral genome packaging; Viral release from host cell.
FT CHAIN 1..641
FT /note="Terminase, large subunit"
FT /id="PRO_0000077673"
FT REGION 1..48
FT /note="Interaction with the terminase small subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144,
FT ECO:0000269|PubMed:2969839"
FT REGION 166..353
FT /note="DNA packaging/ATPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT REGION 166..349
FT /note="DNA packaging/ATPase"
FT /evidence="ECO:0000303|PubMed:17870092,
FT ECO:0000305|PubMed:11866517"
FT REGION 401..586
FT /note="Endonuclease/helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144,
FT ECO:0000269|PubMed:17870092, ECO:0000305|PubMed:1534952"
FT REGION 573..584
FT /note="Basic"
FT /evidence="ECO:0000269|PubMed:1534952"
FT REGION 588..616
FT /note="Leucine zipper"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT REGION 610..641
FT /note="Prohead binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT MOTIF 42..51
FT /note="Q motif"
FT /evidence="ECO:0000269|PubMed:19706522"
FT MOTIF 76..83
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144,
FT ECO:0000269|PubMed:10993723, ECO:0000269|PubMed:19706522,
FT ECO:0000269|PubMed:27139643, ECO:0000269|PubMed:30541105,
FT ECO:0000305|PubMed:9705918"
FT MOTIF 174..179
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144,
FT ECO:0000269|PubMed:30541105"
FT ACT_SITE 179
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144,
FT ECO:0000269|PubMed:30541105"
FT BINDING 401
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT BINDING 491..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144,
FT ECO:0000269|PubMed:8611586, ECO:0000269|PubMed:8794874,
FT ECO:0000269|PubMed:9705918"
FT SITE 46
FT /note="ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144,
FT ECO:0000269|PubMed:10993723"
FT MUTAGEN 18
FT /note="G->E: Lethal, 97% defective in cos cleavage; 84%
FT loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 46
FT /note="Y->A,E: Complete loss of high affinity ATPase
FT activity and packaging; no significant effect on
FT endonuclease or strand separation activities."
FT /evidence="ECO:0000269|PubMed:10993723"
FT MUTAGEN 46
FT /note="Y->F: Complete loss of high affinity ATPase activity
FT and packaging; no significant effect on endonuclease or
FT strand separation activities. 40% decreased velocity of
FT translocation and about 10 times more frequent slipping
FT during DNA translocation."
FT /evidence="ECO:0000269|PubMed:10993723,
FT ECO:0000269|PubMed:19706522"
FT MUTAGEN 76
FT /note="K->A: Complete loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 76
FT /note="K->R: Complete loss of DNA packaging, no effect on
FT cos cleavage, slight increase in strand separation
FT activity."
FT /evidence="ECO:0000269|PubMed:23530228"
FT MUTAGEN 76
FT /note="K->R: Lethal, 85% defective in cos cleavage;
FT complete loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:11866517,
FT ECO:0000269|PubMed:19706522, ECO:0000269|PubMed:27139643"
FT MUTAGEN 77
FT /note="S->V: Complete loss of DNA packaging probably due to
FT a loss of DNA packaging initiation efficiency."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 78
FT /note="A->V: Almost complete loss of DNA packaging; more
FT frequent pausing during packaging."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 79
FT /note="R->A: Complete loss of ATPase and DNA packaging
FT activities."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 79
FT /note="R->K: Almost complete loss of DNA packaging; much
FT lower motor velocity and more frequent pausing during
FT packaging."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 80
FT /note="V->A: Intermediate loss of DNA packaging; more
FT frequent pausing during packaging."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 81
FT /note="G->A: Almost complete loss of DNA packaging; much
FT lower motor velocity."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 82
FT /note="Y->A: Intermediate loss of DNA packaging; much lower
FT motor velocity."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 83
FT /note="S->A: Almost complete loss of ATPase and DNA
FT packaging activities."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 83
FT /note="S->T: Intermediate loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:27139643"
FT MUTAGEN 84
FT /note="K->A: 40% decreased velocity of translocation and
FT 95% loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:19706522"
FT MUTAGEN 84
FT /note="K->E: Complete loss of high affinity ATPase activity
FT and packaging; no significant effect on endonuclease
FT activity and slight decrease in strand separation."
FT /evidence="ECO:0000269|PubMed:10993723"
FT MUTAGEN 166
FT /note="N->Y: Lethal, 95% defective in cos cleavage; almost
FT complete loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 179
FT /note="E->A,Q: Lethal; very weak ATP hydrolysis and
FT complete loss of packaging."
FT /evidence="ECO:0000269|PubMed:30541105"
FT MUTAGEN 179
FT /note="E->C,G,I,L,N,P,R,V: Lethal."
FT /evidence="ECO:0000269|PubMed:30541105"
FT MUTAGEN 179
FT /note="E->D: Lethal; weak ATP hydrolysis and complete loss
FT of packaging, translocation does not seem to be impaired."
FT /evidence="ECO:0000269|PubMed:30541105"
FT MUTAGEN 180
FT /note="L->F: Lethal, 91% defective in cos cleavage; 99%
FT loss of DNA packaging, incomplete packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 191
FT /note="G->S: Lethal, 83% defective in cos cleavage;
FT complete loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 194
FT /note="T->M: Lethal, 66% defective in cos cleavage; 99%
FT loss of DNA packaging, incomplete packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 212
FT /note="G->S: Lethal, 77% defective in cos cleavage; 96%
FT loss of DNA packaging, slow and incomplete packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 225
FT /note="R->H: Lethal, 78% defective in cos cleavage; 84%
FT loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 328
FT /note="T->I: Lethal, 90% defective in cos cleavage; 83%
FT loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 349
FT /note="D->G: Lethal, 89% defective in cos cleavage; 90%
FT loss of DNA packaging."
FT /evidence="ECO:0000269|PubMed:11866517"
FT MUTAGEN 401
FT /note="D->G: Completely defective in cos cleavage."
FT /evidence="ECO:0000269|PubMed:1534952"
FT MUTAGEN 497
FT /note="K->A: Lethal, 1000x reduced cos cleavage, no effect
FT on DNA translocation, increased Km for ATPase to 9.8."
FT /evidence="ECO:0000269|PubMed:8611586,
FT ECO:0000269|PubMed:8794874"
FT MUTAGEN 497
FT /note="K->D: Lethal, 2000x reduced cos cleavage, no effect
FT on DNA translocation, increased Km for ATPase to 24.4."
FT /evidence="ECO:0000269|PubMed:8611586,
FT ECO:0000269|PubMed:8794874"
FT MUTAGEN 497
FT /note="K->R: Km for ATPase increased to 68."
FT /evidence="ECO:0000269|PubMed:8611586"
FT MUTAGEN 586
FT /note="E->K: Completely defective in cos cleavage."
FT /evidence="ECO:0000269|PubMed:1534952"
SQ SEQUENCE 641 AA; 73302 MW; 4C5719C9A2D87B7A CRC64;
MNISNSQVNR LRHFVRAGLR SLFRPEPQTA VEWADANYYL PKESAYQEGR WETLPFQRAI
MNAMGSDYIR EVNVVKSARV GYSKMLLGVY AYFIEHKQRN TLIWLPTDGD AENFMKTHVE
PTIRDIPSLL ALAPWYGKKH RDNTLTMKRF TNGRGFWCLG GKAAKNYREK SVDVAGYDEL
AAFDDDIEQE GSPTFLGDKR IEGSVWPKSI RGSTPKVRGT CQIERAASES PHFMRFHVAC
PHCGEEQYLK FGDKETPFGL KWTPDDPSSV FYLCEHNACV IRQQELDFTD ARYICEKTGI
WTRDGILWFS SSGEEIEPPD SVTFHIWTAY SPFTTWVQIV KDWMKTKGDT GKRKTFVNTT
LGETWEAKIG ERPDAEVMAE RKEHYSAPVP DRVAYLTAGI DSQLDRYEMR VWGWGPGEES
WLIDRQIIMG RHDDEQTLLR VDEAINKTYT RRNGAEMSIS RICWDTGGID PTIVYERSKK
HGLFRVIPIK GASVYGKPVA SMPRKRNKNG VYLTEIGTDT AKEQIYNRFT LTPEGDEPLP
GAVHFPNNPD IFDLTEAQQL TAEEQVEKWV DGRKKILWDS KKRRNEALDC FVYALAALRI
SISRWQLDLS ALLASLQEED GAATNKKTLA DYARALSGED E
