ID A0A3G1LDJ4_9CAUD Unreviewed; 605 AA. AC A0A3G1LDJ4; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 02-OCT-2024, entry version 15. DE RecName: Full=Terminase, large subunit {ECO:0000256|HAMAP-Rule:MF_04144}; DE AltName: Full=DNA-packaging protein {ECO:0000256|HAMAP-Rule:MF_04144}; DE AltName: Full=Large terminase protein {ECO:0000256|HAMAP-Rule:MF_04144}; DE Includes: DE RecName: Full=Endonuclease {ECO:0000256|HAMAP-Rule:MF_04144}; DE EC=3.1.21.4 {ECO:0000256|HAMAP-Rule:MF_04144}; DE Includes: DE RecName: Full=Helicase {ECO:0000256|HAMAP-Rule:MF_04144}; DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_04144}; DE Includes: DE RecName: Full=ATPase {ECO:0000256|HAMAP-Rule:MF_04144}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04144}; GN ORFNames=HSA30_gp001 {ECO:0000313|EMBL:AUG85505.1}; OS Staphylococcus phage HSA30. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Herelleviridae; Twortvirinae; Kayvirus; Kayvirus P108. OX NCBI_TaxID=2054877 {ECO:0000313|EMBL:AUG85505.1, ECO:0000313|Proteomes:UP000271715}; RN [1] {ECO:0000313|EMBL:AUG85505.1, ECO:0000313|Proteomes:UP000271715} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Seo H.S., Na H., Ryu S.; RT "Complete genome of Staphylococcus aureus bacteriophage HSA30."; RL Submitted (NOV-2017) 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 from the concetamer to CC initiate and to end the packaging reaction. The terminase lies at a CC unique vertex of the procapsid and is composed of two subunits, a small CC terminase subunit involved in viral DNA recognition, and a large CC terminase subunit possessing endonucleolytic, ATPase and helicase CC activities (DNA maturation and packaging). The endonuclease activity CC cleaves the viral DNA generating 5'overhangs. The helicase activity CC separates the cohesive ends generating the single-stranded 'sticky' CC ends of the mature genome. The DNA-terminase complex binds to the CC portal of the procapsid thereby activating the translocase activity of CC the terminase. The terminase packages the viral DNA into the procapsid CC until the next concatemer reaches the complex. The downstream site is CC then cut generating the mature right end of the genome, the CC heterotrimer undocks from the DNA-filled head and remains bound to the CC left end of concatemer's next genome. {ECO:0000256|HAMAP- CC Rule:MF_04144}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04144}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of DNA to give specific double- CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; CC Evidence={ECO:0000256|HAMAP-Rule:MF_04144}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_04144}; CC -!- SUBUNIT: Interacts (via N-terminus) with the terminase small subunit CC (via C-terminus); the active complex is probably heterooligomeric. CC Interacts (via C-terminus) with the portal protein; this interaction CC allows the packaging of viral DNA. {ECO:0000256|HAMAP-Rule:MF_04144}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04144}. CC Note=The terminase lies at a unique vertex of the procapsid during CC viral DNA packaging. {ECO:0000256|HAMAP-Rule:MF_04144}. CC -!- DOMAIN: The N-terminus is involved in the formation of the heterotrimer CC with the small subunit. The N-terminus part contains the translocase CC activity involved in DNA packaging. At the N-terminus, there is a high CC affinity ATPase center that is probably needed for the packaging CC activity. The Walker A motif of the ATPase center is responsible for CC interacting with the ATP phosphate and the Q motif governs force CC generation and the interaction with DNA. The C-terminus contains the CC site specific endonuclease (cos-cleavage) and strand separation CC (helicase) activities required for genome maturation. A second ATPase CC catalytic site regulates the genome maturation. The C-terminus very end CC is involved in binding to the procapsid. Contains a basic leucine CC zipper (bZIP) that may be involved in the formation of the terminase. CC {ECO:0000256|HAMAP-Rule:MF_04144}. CC -!- SIMILARITY: Belongs to the lambdavirus large terminase family. CC {ECO:0000256|HAMAP-Rule:MF_04144}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04144}. 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; MG557618; AUG85505.1; -; Genomic_DNA. DR Proteomes; UP000271715; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0098009; C:viral terminase, large subunit; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule. DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_04144; TERL_LAMBDA; 1. DR InterPro; IPR046453; GpA_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008866; Phage_lambda_GpA-like. DR Pfam; PF05876; GpA_ATPase; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04144}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_04144}; KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04144}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04144}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04144}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04144}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_04144}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04144}; KW Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04144}; KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04144}. FT DOMAIN 79..287 FT /note="Phage terminase large subunit GpA ATPase" FT /evidence="ECO:0000259|Pfam:PF05876" FT MOTIF 82..89 FT /note="Walker A motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04144" FT MOTIF 176..181 FT /note="Walker B motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04144" FT ACT_SITE 181 FT /note="For ATPase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04144" FT BINDING 390 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic; for nuclease activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04144" SQ SEQUENCE 605 AA; 70256 MW; 3EDE0D131546E5AC CRC64; MDGKELIKIA QETFQTEKIT REQIDHIINM LNPSTYMLKY HTLRGHPITF SIPNRDRSKA QAHRPWQTRI VNDTHPNKAV IKSRQLGLSE MGVMEMVHFA DMHSYANAKC LYTFPTNEQM KKFVQSRLNP VLEKEYFRDI VDWDKDSLGF KKIRNSSLFF RTSSKASTVE GVDIDYLSLD EYDRVNLLAE SSALESMSSS PFKIVRRWST PSVPGMGIHK LYQQSDQWYY GHRCQHCDYL NEMSYNDYNP DNLEESGNML CVNPEGVDEQ AKTVQNGSYQ FVCQKCGKPL DRWYNGEWHC KYPERTKGNK GVRGYLITQM NAVWISADEL KEKEMNTESK QAFYNYILGY PFEDVKLRVN EEDVYGNKSP IAETQLMKRD RYSHIAIGID WGNTHWITVH GMLPNGKVDL IRLFSVKKMT RPDLVEADLE KIIWEISKYD PDIIIADNGD SGNNVLKLIN HFGKDKVFGC TYKSSPKSTG QLRPEFNENN NRVTVDKLMQ NKRYIQALKT KDISVYSTVD DDLKTFLKHW QNVVIMDEED EKTGEMYQVI KRKGDDHYAQ ASVYAYIGLT RIKELLKEGN GTSFGSTFVS TDYNQEGNKQ FYFDE //