ID A1BU51_9CAUD Unreviewed; 446 AA.
AC A1BU51;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 08-NOV-2023, entry version 45.
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=ph2 {ECO:0000313|EMBL:ABI21779.1};
OS Rockefellervirus PH15.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Rockefellervirus.
OX NCBI_TaxID=399185 {ECO:0000313|EMBL:ABI21779.1, ECO:0000313|Proteomes:UP000006925};
RN [1] {ECO:0000313|EMBL:ABI21779.1, ECO:0000313|Proteomes:UP000006925}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PH15 {ECO:0000313|EMBL:ABI21779.1};
RX PubMed=17172342; DOI=10.1128/JB.01637-06;
RA Daniel A., Bonnen P.E., Fischetti V.A.;
RT "First complete genome sequence of two Staphylococcus epidermidis
RT bacteriophages.";
RL J. Bacteriol. 189:2086-2100(2007).
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 -!- 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04145}.
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DR EMBL; DQ834250; ABI21779.1; -; Genomic_DNA.
DR RefSeq; YP_950664.1; NC_008723.1.
DR GeneID; 4643176; -.
DR KEGG; vg:4643176; -.
DR OrthoDB; 2120at10239; -.
DR Proteomes; UP000006925; Segment.
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 Nuclease {ECO:0000256|HAMAP-Rule:MF_04145};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04145};
KW Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04145};
KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04145}.
FT DOMAIN 28..231
FT /note="Phage terminase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04466"
FT DOMAIN 296..434
FT /note="Phage terminase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17288"
FT MOTIF 33..40
FT /note="Walker A motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT MOTIF 130..135
FT /note="Walker B motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT ACT_SITE 135
FT /note="For ATPase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
SQ SEQUENCE 446 AA; 51837 MW; 0D63F883BAB8B014 CRC64;
MISIKLSELL PKHFHSLWKA TKDREKLNIV AKGGRGSGKS SDISIIITQL IMRYPMNAVV
VRKADNTLAT SVFEQIKWAI EEQKVSHLFK VKVSPMEITY VPRGNRIIFR GAQNPERLKS
LKDSRFPFSI MWIEELAEFK TEDEVTTITN SMLRGELDDG LFYKFFFSYN PPKRKQSWVN
KKYETSFQPD NTFVHHSTYL DNPFISKQFI QEAESAKERN EQRYRWEYMG EAIGSGVVPF
NNLQIEKIPD ELYKSFDNIR NAVDFGLTKT APLHSDVYSK LGEHISGVRK KACATDPLAF
VRWHYDKKKR IIYAVDEHYG VQISNREFAN WLKRRGYQSD EIYADSAEPK SIAELKQEHG
IKRIKGVKKG PDSVEHGEQW LDDLTAIVID PNRTPNIARE FENIDYETDK DGNVKPRLED
KDNHTIDATR YALERDMRQN KLSILT
//
