TERL_BPSPP
ID TERL_BPSPP Reviewed; 422 AA.
AC P54308;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04145};
DE AltName: Full=DNA-packaging protein {ECO:0000255|HAMAP-Rule:MF_04145};
DE AltName: Full=Gene product 2;
DE Short=gp2;
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04145};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04145, ECO:0000269|PubMed:10930407, ECO:0000269|PubMed:12697751, ECO:0000269|PubMed:19444313, ECO:0000269|PubMed:23118480};
DE Includes:
DE RecName: Full=ATPase {ECO:0000255|HAMAP-Rule:MF_04145};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04145, ECO:0000269|PubMed:10930407, ECO:0000269|PubMed:12697751};
GN Name=2;
OS Bacillus phage SPP1 (Bacteriophage SPP1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=10724;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1548711; DOI=10.1016/0022-2836(92)90578-8;
RA Chai S., Bravo A., Lueder G., Nedlin A., Trautner T.A., Alonso J.C.;
RT "Molecular analysis of the Bacillus subtilis bacteriophage SPP1 region
RT encompassing genes 1 to 6. The products of gene 1 and gene 2 are required
RT for pac cleavage.";
RL J. Mol. Biol. 224:87-102(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9434185; DOI=10.1016/s0378-1119(97)00547-7;
RA Alonso J.C., Luder G., Stiege A.C., Chai S., Weise F., Trautner T.A.;
RT "The complete nucleotide sequence and functional organization of Bacillus
RT subtilis bacteriophage SPP1.";
RL Gene 204:201-212(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30544981; DOI=10.3390/v10120705;
RA Godinho L.M., El Sadek Fadel M., Monniot C., Jakutyte L., Auzat I.,
RA Labarde A., Djacem K., Oliveira L., Carballido-Lopez R., Ayora S.,
RA Tavares P.;
RT "The revisited genome of Bacillus subtilis bacteriophage SPP1.";
RL Viruses 10:0-0(2018).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=10930407; DOI=10.1074/jbc.m004309200;
RA Gual A., Camacho A.G., Alonso J.C.;
RT "Functional analysis of the terminase large subunit, G2P, of Bacillus
RT subtilis bacteriophage SPP1.";
RL J. Biol. Chem. 275:35311-35319(2000).
RN [5]
RP SUBUNIT, CATALYTIC ACTIVITY, INTERACTION WITH GP1, AND INTERACTION WITH THE
RP PORTAL PROTEIN.
RX PubMed=12697751; DOI=10.1074/jbc.m301805200;
RA Camacho A.G., Gual A., Lurz R., Tavares P., Alonso J.C.;
RT "Bacillus subtilis bacteriophage SPP1 DNA packaging motor requires
RT terminase and portal proteins.";
RL J. Biol. Chem. 278:23251-23259(2003).
RN [6]
RP DOMAIN.
RX PubMed=16377618; DOI=10.1074/jbc.m511817200;
RA Ponchon L., Boulanger P., Labesse G., Letellier L.;
RT "The endonuclease domain of bacteriophage terminases belongs to the
RT resolvase/integrase/ribonuclease H superfamily: a bioinformatics analysis
RT validated by a functional study on bacteriophage T5.";
RL J. Biol. Chem. 281:5829-5836(2006).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=23419885; DOI=10.1016/j.virusres.2013.01.021;
RA Oliveira L., Tavares P., Alonso J.C.;
RT "Headful DNA packaging: bacteriophage SPP1 as a model system.";
RL Virus Res. 173:247-259(2013).
RN [9]
RP COFACTOR, CATALYTIC ACTIVITY, AND INTERACTION WITH THE PORTAL PROTEIN.
RX PubMed=23118480; DOI=10.1093/nar/gks974;
RA Cornilleau C., Atmane N., Jacquet E., Smits C., Alonso J.C., Tavares P.,
RA Oliveira L.;
RT "The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage
RT and encapsidation.";
RL Nucleic Acids Res. 41:340-354(2013).
RN [10] {ECO:0007744|PDB:2WBN, ECO:0007744|PDB:2WC9}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 232-422 IN COMPLEX WITH
RP MANGANESE, MUTAGENESIS OF ASP-266; ASP-321; HIS-400 AND ASP-403, COFACTOR,
RP AND CATALYTIC ACTIVITY.
RX PubMed=19444313; DOI=10.1038/embor.2009.53;
RA Smits C., Chechik M., Kovalevskiy O.V., Shevtsov M.B., Foster A.W.,
RA Alonso J.C., Antson A.A.;
RT "Structural basis for the nuclease activity of a bacteriophage large
RT terminase.";
RL EMBO Rep. 10:592-598(2009).
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 (PubMed:10930407). 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 (PubMed:23419885). Both terminase subunits
CC heterooligomerize and are docked on the portal protein to form the
CC packaging machine (PubMed:23419885). The terminase large subunit
CC exhibits endonuclease activity and cleaves the viral genome concatemer
CC once the capsid is full (headful packaging) (Probable)
CC (PubMed:10930407). Once the capsid is packaged with the DNA, the
CC terminase complex is substituted by the adapter (gp15) and the stopper
CC protein (gp16) that form the connector (Probable). {ECO:0000255|HAMAP-
CC Rule:MF_04145, ECO:0000269|PubMed:10930407,
CC ECO:0000269|PubMed:23419885, ECO:0000305|PubMed:23419885}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04145,
CC ECO:0000269|PubMed:19444313};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04145,
CC ECO:0000269|PubMed:10930407};
CC Note=Binds 2 divalent metal cations per subunit. Mn(2+) is preferred
CC over Mg(2+) (By similarity). Optimum concentration of Mg(2+) is 10 mm
CC (PubMed:10930407). As the Mn(2+) dose increases, gp2 converts
CC supercoiled circular plasmid DNA to nicked open circular DNA,
CC subsequently to linear DNA and finally to completely degraded DNA
CC (PubMed:19444313). {ECO:0000255|HAMAP-Rule:MF_04145,
CC ECO:0000269|PubMed:10930407, ECO:0000269|PubMed:19444313};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:10930407};
CC -!- SUBUNIT: Monomer. Interacts with the terminase small subunit; the
CC active complex is probably composed of two decameric ring-shaped
CC terminase small subunit and two monomeric terminase large subunit
CC (PubMed:12697751). Interacts with the portal protein (PubMed:23118480,
CC PubMed:12697751). {ECO:0000255|HAMAP-Rule:MF_04145,
CC ECO:0000269|PubMed:12697751, ECO:0000269|PubMed:23118480}.
CC -!- DOMAIN: The N-terminus contains an ATPase domain and the C-terminus
CC contains an endonuclease domain. {ECO:0000255|HAMAP-Rule:MF_04145,
CC ECO:0000269|PubMed:16377618}.
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; X56064; CAA39537.1; -; Genomic_DNA.
DR EMBL; X97918; CAA66573.1; -; Genomic_DNA.
DR PIR; S24451; S24451.
DR RefSeq; NP_690654.1; NC_004166.2.
DR PDB; 2WBN; X-ray; 1.90 A; A=232-422.
DR PDB; 2WC9; X-ray; 2.50 A; A=232-422.
DR PDBsum; 2WBN; -.
DR PDBsum; 2WC9; -.
DR SMR; P54308; -.
DR PRIDE; P54308; -.
DR GeneID; 955254; -.
DR KEGG; vg:955254; -.
DR EvolutionaryTrace; P54308; -.
DR Proteomes; UP000002559; 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; 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:0004518; F:nuclease activity; IDA:UniProtKB.
DR GO; GO:0019073; P:viral DNA genome packaging; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04145; TERL_SPP1; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006437; Phage_terminase_lsu.
DR InterPro; IPR035413; Terminase_L_C.
DR InterPro; IPR035412; Terminase_L_N.
DR InterPro; IPR044269; Terminase_large_su_SPP1-like.
DR Pfam; PF04466; Terminase_3; 1.
DR Pfam; PF17288; Terminase_3C; 1.
DR TIGRFAMs; TIGR01547; phage_term_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endonuclease; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nuclease; Nucleotide-binding; Reference proteome;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..422
FT /note="Terminase, large subunit"
FT /id="PRO_0000077789"
FT REGION 1..198
FT /note="ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:16377618, ECO:0000269|PubMed:23118480"
FT REGION 232..422
FT /note="Nuclease activity and binding to the portal protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:16377618, ECO:0000269|PubMed:23118480"
FT MOTIF 33..40
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:16377618"
FT MOTIF 130..135
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:16377618"
FT ACT_SITE 135
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:19444313"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:19444313"
FT BINDING 321
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:19444313"
FT BINDING 400
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:19444313"
FT BINDING 403
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04145,
FT ECO:0000269|PubMed:19444313"
FT VARIANT 18
FT /note="W -> R (in isolate Ts6M; temperature-sensitive)"
FT VARIANT 73
FT /note="F -> L (in isolate SUS19)"
FT VARIANT 233
FT /note="L -> F (in isolate SUS19)"
FT VARIANT 412
FT /note="D -> N (in isolate Ts10M; temperature-sensitive)"
FT MUTAGEN 266
FT /note="D->N: Complete loss of endonuclease activity."
FT MUTAGEN 321
FT /note="D->N: Complete loss of endonuclease activity."
FT MUTAGEN 400
FT /note="H->A: Decreased endonuclease activity."
FT MUTAGEN 403
FT /note="D->N: Complete loss of endonuclease activity."
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2WBN"
FT HELIX 252..257
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 274..282
FT /evidence="ECO:0007829|PDB:2WBN"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:2WBN"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2WBN"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:2WBN"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:2WBN"
FT HELIX 350..358
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:2WBN"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:2WBN"
FT HELIX 371..379
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2WC9"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:2WBN"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2WBN"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:2WBN"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:2WBN"
SQ SEQUENCE 422 AA; 48841 MW; 55D16BDB32239A5C CRC64;
MKKVRLSEKF TPHFLEVWRT VKAAQHLKYV LKGGRGSAKS THIAMWIILL MMMMPITFLV
IRRVYNTVEQ SVFEQLKEAI DMLEVGHLWK VSKSPLRLTY IPRGNSIIFR GGDDVQKIKS
IKASKFPVAG MWIEELAEFK TEEEVSVIEK SVLRAELPPG CRYIFFYSYN PPKRKQSWVN
KVFNSSFLPA NTFVDHSTYL QNPFLSKAFI EEAEEVKRRN ELKYRHEYLG EALGSGVVPF
ENLQIEEGII TDAEVARFDN IRQGLDFGYG PDPLAFVRWH YDKRKNRIYA IDELVDHKVS
LKRTADFVRK NKYESARIIA DSSEPRSIDA LKLEHGINRI EGAKKGPDSV EHGERWLDEL
DAIVIDPLRT PNIAREFENI DYQTDKNGDP IPRLEDKDNH TIDATRYAFE RDMKKGGVSL
WG
