ID A0A4D5ZZ98_9CAUD Unreviewed; 435 AA.
AC A0A4D5ZZ98;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Terminase, large subunit {ECO:0000256|HAMAP-Rule:MF_04145};
DE AltName: Full=DNA-packaging protein {ECO:0000256|HAMAP-Rule:MF_04145};
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000256|HAMAP-Rule:MF_04145};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_04145};
DE Includes:
DE RecName: Full=ATPase {ECO:0000256|HAMAP-Rule:MF_04145};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04145};
GN ORFNames=Javan119_0036 {ECO:0000313|EMBL:QBX14074.1};
OS Streptococcus phage Javan119.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=2547988 {ECO:0000313|EMBL:QBX14074.1, ECO:0000313|Proteomes:UP000296824};
RN [1] {ECO:0000313|Proteomes:UP000296824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Rezaei Javan R., Ramos-Sevillano E., Akter A., Brown J., Brueggemann A.B.;
RT "Prophages and satellite prophages are widespread among Streptococcus
RT species and may play a role in pneumococcal pathogenesis.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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 Both terminase subunits heterooligomerize and are docked on the portal
CC protein to form the packaging machine. The terminase large subunit
CC exhibits endonuclease activity and cleaves the viral genome concatemer
CC once the capsid is full (headful packaging). Once the capsid is
CC packaged with the DNA, the terminase complex is substituted by the
CC adapter and the stopper protein that form the connector.
CC {ECO:0000256|HAMAP-Rule:MF_04145}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04145};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04145};
CC Note=Binds 2 divalent metal cations per subunit. Mn(2+) is preferred
CC over Mg(2+). {ECO:0000256|HAMAP-Rule:MF_04145};
CC -!- SUBUNIT: Monomer. Interacts with the terminase small subunit; the
CC active complex is probably heterooligomeric. Interacts with the portal
CC protein. {ECO:0000256|HAMAP-Rule:MF_04145}.
CC -!- DOMAIN: The N-terminus contains an ATPase domain and the C-terminus
CC contains an endonuclease domain. {ECO:0000256|HAMAP-Rule:MF_04145}.
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DR EMBL; MK448673; QBX14074.1; -; Genomic_DNA.
DR Proteomes; UP000296824; Genome.
DR GO; GO:0098009; C:viral terminase, large subunit; IEA:UniProtKB-UniRule.
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:0051276; P:chromosome organization; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.420.280; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01547; phage_term_2; 1.
DR PANTHER; PTHR39184; -; 1.
DR PANTHER; PTHR39184:SF1; PBSX PHAGE TERMINASE LARGE SUBUNIT; 1.
DR Pfam; PF04466; Terminase_3; 1.
DR Pfam; PF17288; Terminase_3C; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04145};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_04145};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04145};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04145};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_04145};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04145};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_04145};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04145};
KW Reference proteome {ECO:0000313|Proteomes:UP000296824};
KW Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04145};
KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04145}.
FT DOMAIN 33..239
FT /note="Phage terminase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04466"
FT DOMAIN 273..414
FT /note="Phage terminase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17288"
FT MOTIF 40..47
FT /note="Walker A motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT MOTIF 138..143
FT /note="Walker B motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT ACT_SITE 143
FT /note="For ATPase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT BINDING 328
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT BINDING 404
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT BINDING 407
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
SQ SEQUENCE 435 AA; 50752 MW; 3CFA9EDC997077F3 CRC64;
MKTTYQTKPK LEIKVDLPKT IGIGYGDFWR SRNFYRVVKG SRGSKKSKTT ALNFVVRLLK
YEWANLLVIR RYSNTNKQST YTDFKWACNQ LKVSHLFKFN ESLPEITVKA TGQKILFRGL
DDELKITSIT VDVGALCWAW FEEAYQIETE DKFSTVVESI RGTLDVPDFF KQITVTFNPW
SERHWLKRVF FDEETKRADT FSGTTTFRVN EWLDDVDKRR YEDLYKTNPR RARIVCDGEW
GVAEGLVFDN FEVVDFDVEK TIQRIKETSA GMDFGFTQDP TTLICVAVDL ANKELWLYNE
HYQKAMLTDH IVKMIRDKNL HRSYIAGDSA EKRLIAEIKS KGVSGIVPSI KGKGSIMQGI
QFMQGFKIHI HPSCEHTIEE FNTYTFKQDK EGNWLNEPID KNNHVIDAIR YALEKYHIRS
NESNQFEVLR QGFGY
//
