ID Q4ZAI3_9CAUD Unreviewed; 421 AA.
AC Q4ZAI3;
DT 07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2005, sequence version 1.
DT 08-NOV-2023, entry version 40.
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};
OS Staphylococcus phage 92.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Azeredovirinae; Phietavirus; Phietavirus pv92.
OX NCBI_TaxID=2908151 {ECO:0000313|EMBL:AAX91940.1, ECO:0000313|Proteomes:UP000001463};
RN [1] {ECO:0000313|EMBL:AAX91940.1, ECO:0000313|Proteomes:UP000001463}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15788529; DOI=10.1073/pnas.0501140102;
RA Kwan T., Liu J., Dubow M., Gros P., Pelletier J.;
RT "The complete genomes and proteomes of 27 Staphylococcus aureus
RT bacteriophages.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5174-5179(2005).
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}.
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; AY954967; AAX91940.1; -; Genomic_DNA.
DR RefSeq; YP_240743.1; NC_007064.1.
DR GeneID; 5133804; -.
DR KEGG; vg:5133804; -.
DR OrthoDB; 2120at10239; -.
DR Proteomes; UP000001463; 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 Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04145};
KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04145}.
FT DOMAIN 31..232
FT /note="Phage terminase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04466"
FT DOMAIN 265..409
FT /note="Phage terminase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17288"
FT MOTIF 34..41
FT /note="Walker A motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT MOTIF 131..136
FT /note="Walker B motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT ACT_SITE 136
FT /note="For ATPase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04145"
FT BINDING 265
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 265
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 320
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 399
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 402
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 421 AA; 49183 MW; EEBB6FEDF29A7BAC CRC64;
MTISINLSDL LPKHFHPLWK VTKDKEVLNV VAKGGRGSGK SSDISIIITQ LIMRYPMNAV
VIRKTDNTLA TSVFEQIKWA IEEQKVSHLF KVKVSPMEIT YIPRGNRIIF RGAQNPERLK
SLKDSRFPFS IAWIEELAEF KTEDEVTTIT NSLLRGELDE GLFYKFFFSY NPPKRKQSWV
NKKYESSFQA DNTYVHHSTY LNNPFISKQF IQEAESAKKR NEQRYRWEYM GEAIGSGVVP
FNNLRIEEIP QRQYDTFDNI RNAVDFGYAT DPLAFVRWHY DKKKRVIYAM DEYYGVQISN
REFANWLKKK GYQSDEIFAD SAEPKSIAEL KQEHGIKKIK GVKKGADSVE FGEQWLDDLD
AIVIDPRRTP NIAREFENID YETDKDGNVK PKLEDKDNHT IDATRYALER DMRQNKLSIL
R
//
