TERL_BPP22
ID TERL_BPP22 Reviewed; 499 AA.
AC P26745; Q7PCJ5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04148, ECO:0000303|PubMed:26301600};
DE AltName: Full=DNA-packaging protein gp2 {ECO:0000255|HAMAP-Rule:MF_04148};
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04148};
DE EC=3.1.21.- {ECO:0000255|HAMAP-Rule:MF_04148, ECO:0000269|PubMed:22715098};
DE Includes:
DE RecName: Full=ATPase {ECO:0000255|HAMAP-Rule:MF_04148};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04148, ECO:0000269|PubMed:22771211};
GN Name=2;
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], AND PROTEIN SEQUENCE OF 1-8.
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 [2]
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 [3]
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 [4]
RP INTERACTION WITH THE TERMINASE SMALL SUBUNIT, AND SUBUNIT.
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 [5]
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 [6]
RP CATALYTIC ACTIVITY, 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).
RN [7]
RP INTERACTION WITH THE TERMINASE SMALL SUBUNIT, SUBUNIT, AND DOMAIN.
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 [8]
RP INTERACTION WITH THE PORTAL PROTEIN.
RX PubMed=28134243; DOI=10.1038/ncomms14310;
RA Lokareddy R.K., Sankhala R.S., Roy A., Afonine P.V., Motwani T.,
RA Teschke C.M., Parent K.N., Cingolani G.;
RT "Portal protein functions akin to a DNA-sensor that couples genome-
RT packaging to icosahedral capsid maturation.";
RL Nat. Commun. 8:14310-14310(2017).
RN [9] {ECO:0007744|PDB:4DKW}
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 289-499, COFACTOR, SUBUNIT,
RP DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=22715098; DOI=10.1074/jbc.m112.349894;
RA Roy A., Cingolani G.;
RT "Structure of p22 headful packaging nuclease.";
RL J. Biol. Chem. 287:28196-28205(2012).
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 to initiate and to end a
CC packaging reaction. 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 (packaging sequence), and a large
CC terminase subunit possessing endonucleolytic and ATPase activities
CC (Probable). Both terminase subunits heterooligomerize and are docked on
CC the portal protein to form the packaging machine (PubMed:22771211).
CC Once the capsid is packaged with the DNA (headful packaging), the
CC terminase cleaves the viral genome concatemer and is substituted by the
CC tail (Probable). {ECO:0000255|HAMAP-Rule:MF_04148,
CC ECO:0000269|PubMed:22771211, ECO:0000305|PubMed:22771211}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04148,
CC ECO:0000269|PubMed:22715098};
CC Note=Nuclease activity probably requires 2 Mg(2+) ions per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_04148, ECO:0000269|PubMed:22715098};
CC -!- SUBUNIT: Interacts with the terminase small subunit; the active complex
CC is composed of a monomer of the terminase large subunit and a nonamer
CC ring of terminase small subunits (PubMed:17945256, PubMed:26301600)
CC (Probable). Interacts with the portal protein; this interaction allows
CC the packaging of viral DNA (PubMed:28134243). {ECO:0000255|HAMAP-
CC Rule:MF_04148, ECO:0000269|PubMed:17945256,
CC ECO:0000269|PubMed:26301600, ECO:0000269|PubMed:28134243,
CC ECO:0000305|PubMed:22715098}.
CC -!- DOMAIN: The ATPase region is in the N-terminus, whereas the nuclease
CC region is in the C-terminus. {ECO:0000255|HAMAP-Rule:MF_04148,
CC ECO:0000269|PubMed:22715098, ECO:0000269|PubMed:26301600}.
CC -!- SIMILARITY: Belongs to the Lederbergvirus large terminase family.
CC {ECO:0000255|HAMAP-Rule:MF_04148}.
CC -!- CAUTION: His-326 has proposed to bind the second magnesium, but this is
CC not in accordance with the sites identified in phage G20c and Thermus
CC thermophilus RuvC, and with the mutagenesis results in phage T4.
CC {ECO:0000305|PubMed:22715098}.
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DR EMBL; M59749; AAA72959.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75044.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA00977.1; -; Genomic_DNA.
DR PIR; B40474; Z2BP22.
DR RefSeq; YP_063734.1; NC_002371.2.
DR PDB; 4DKW; X-ray; 2.02 A; A/B/C/D=289-499.
DR PDB; 6VI1; X-ray; 2.40 A; M/N/O/P/Q/R=1-33.
DR PDB; 6XMI; X-ray; 1.51 A; C/F=1-33.
DR PDBsum; 4DKW; -.
DR PDBsum; 6VI1; -.
DR PDBsum; 6XMI; -.
DR SMR; P26745; -.
DR DIP; DIP-59856N; -.
DR IntAct; P26745; 1.
DR ABCD; P26745; 1 sequenced antibody.
DR GeneID; 2944239; -.
DR KEGG; vg:2944239; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; Genome.
DR GO; GO:0043493; C:viral terminase complex; IDA:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04148; TERL_BPP22; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035421; Terminase_6C.
DR InterPro; IPR044265; Terminase_large_su_BPP22.
DR Pfam; PF17289; Terminase_6C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Endonuclease;
KW Hydrolase; Late protein; Magnesium; Metal-binding; Nuclease;
KW Nucleotide-binding; Reference proteome; Viral genome packaging;
KW Viral release from host cell.
FT CHAIN 1..499
FT /note="Terminase, large subunit"
FT /id="PRO_0000077749"
FT REGION 1..286
FT /note="ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04148,
FT ECO:0000269|PubMed:22715098, ECO:0000269|PubMed:26301600"
FT REGION 1..58
FT /note="Interaction with the terminase small subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04148,
FT ECO:0000269|PubMed:26301600"
FT REGION 312..482
FT /note="Nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04148,
FT ECO:0000269|PubMed:22715098, ECO:0000269|PubMed:26301600"
FT MOTIF 60..67
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04148"
FT MOTIF 199..204
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04148"
FT ACT_SITE 204
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04148"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04148,
FT ECO:0000269|PubMed:22715098"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04148,
FT ECO:0000269|PubMed:22715098"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:6XMI"
FT HELIX 12..31
FT /evidence="ECO:0007829|PDB:6XMI"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4DKW"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:4DKW"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:4DKW"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4DKW"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:4DKW"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:4DKW"
FT STRAND 341..352
FT /evidence="ECO:0007829|PDB:4DKW"
FT HELIX 355..366
FT /evidence="ECO:0007829|PDB:4DKW"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:4DKW"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:4DKW"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:4DKW"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:4DKW"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:4DKW"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:4DKW"
FT HELIX 459..469
FT /evidence="ECO:0007829|PDB:4DKW"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:4DKW"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:4DKW"
SQ SEQUENCE 499 AA; 57592 MW; 6E8FE06F43182C39 CRC64;
MELDAILDNL SDEEQIELLE LLEEEENYRN THLLYEFAPY SKQREFIDAG HDYPERCFMA
GNQLGKSFTG AAEVAFHLTG RYPGTKGYPA DGKYGGEWKG KRFYEPVVFW IGGETNETVT
KTTQRILCGR IEENDEPGYG SIPKEDIISW KKSPFFPNLV DHLLVKHHTA DGVEDGISIC
YFKPYSQGRA RWQGDTIHGV WFDEEPPYSI YGEGLTRTNK YGQFSILTFT PLMGMSDVVT
KFLKNPSKSQ KVVNMTIYDA EHYTDEQKEQ IIASYPEHER EARARGIPTM GSGRIFQIPE
ETIKCQPFEC PDHFYVIDAQ DFGWNHPQAH IQLWWDKDAD VFYLARVWKK SENTAVQAWG
AVKSWANKIP VAWPHDGHQH EKGGGEQLKT QYADAGFSML PDHATFPDGG NSVESGISEL
RDLMLEGRFK VFNTCEPFFE EFRLYHRDEN GKIVKTNDDV LDATRYGYMM RRFARMMRDI
RKPKEKKIPA PIRPVRRGR
