ID I6WKD1_9CAUD Unreviewed; 605 AA.
AC I6WKD1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 Name=ter {ECO:0000313|EMBL:AFN38518.1};
GN ORFNames=phi_Fi200W_ter {ECO:0000313|EMBL:AFN38518.1};
OS Staphylococcus phage Fi200W.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Herelleviridae; Twortvirinae; Kayvirus; Kayvirus G1.
OX NCBI_TaxID=1195078 {ECO:0000313|EMBL:AFN38518.1, ECO:0000313|Proteomes:UP000224692};
RN [1] {ECO:0000313|EMBL:AFN38518.1, ECO:0000313|Proteomes:UP000224692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22748811; DOI=10.1016/B978-0-12-394438-2.00005-0;
RA Lobocka M., Hejnowicz M.S., Dabrowski K., Gozdek A., Kosakowski J.,
RA Witkowska M., Ulatowska M.I., Weber-Dabrowska B., Kwiatek M., Parasion S.,
RA Gawor J., Kosowska H., Glowacka A.;
RT "Genomics of Staphylococcal Twort-like Phages - Potential Therapeutics of
RT the Post-Antibiotic Era.";
RL Adv. Virus Res. 83:143-216(2012).
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}.
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DR EMBL; JX080303; AFN38518.1; -; Genomic_DNA.
DR Proteomes; UP000224692; 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..265
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; 70242 MW; 1C543C8006ED6614 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 NKRYVQALKT KDISVYSTVD DDLKTFLKHW QNVVIMDEED
EKTGEMYQVI KRKGDDHYAQ ASVYAYIGLT RIKELLKEGN GTSFGSTFVS TDYNQEGNKQ
FYFDE
//
