TERL_BPMU
ID TERL_BPMU Reviewed; 551 AA.
AC Q9T1W6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 23-FEB-2022, entry version 70.
DE RecName: Full=Probable terminase, large subunit gp28;
DE EC=3.1.-.- {ECO:0000305};
DE AltName: Full=Gene product 28;
DE Short=gp28;
DE AltName: Full=Gene product E;
DE Short=gpE;
DE AltName: Full=Pacase, large subunit;
DE AltName: Full=Packaging protein E;
GN OrderedLocusNames=Mup28;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [2]
RP INDUCTION.
RX PubMed=8293968; DOI=10.1093/genetics/135.3.619;
RA Chiang L.W., Howe M.M.;
RT "Mutational analysis of a C-dependent late promoter of bacteriophage Mu.";
RL Genetics 135:619-629(1993).
RN [3]
RP IDENTIFICATION.
RX PubMed=14745593; DOI=10.1007/s00705-003-0216-4;
RA Siboo I.R., Sieder F., Kumar K., Howe M.M., DuBow M.S.;
RT "Characterization of Plys-proximal morphogenetic genes of transposable
RT bacteriophage Mu.";
RL Arch. Virol. 149:241-259(2004).
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 neck
CC proteins. {ECO:0000250|UniProtKB:P17312}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P17312};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P17312};
CC -!- SUBUNIT: Interacts with the terminase small subunit gp28.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC Expression of late genes is activated by the viral late transcription
CC activator C. {ECO:0000269|PubMed:8293968}.
CC -!- SIMILARITY: Belongs to the T4likevirus large terminase family.
CC {ECO:0000305}.
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DR EMBL; AF083977; AAF01106.1; -; Genomic_DNA.
DR RefSeq; NP_050632.1; NC_000929.1.
DR GeneID; 2636303; -.
DR KEGG; vg:2636303; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032359; P:provirus excision; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012036; Phage_Mu_Gp28.
DR PIRSF; PIRSF007056; UCP007056; 1.
PE 2: Evidence at transcript level;
KW Endonuclease; Host cytoplasm; Hydrolase; Late protein; Magnesium;
KW Metal-binding; Nuclease; Reference proteome; Viral genome excision;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..551
FT /note="Probable terminase, large subunit gp28"
FT /id="PRO_0000077822"
SQ SEQUENCE 551 AA; 62636 MW; B63D646144653A7C CRC64;
MNTRENNLKA LHAPRKINLR EEAGLLGVDI VTDIGEAQPR NEPVFLGYQR RWFEDESQIC
IAEKSRRTGL TWAEAGRNVM TAAKPKRRGG RNVFYVGSRQ EMALEYIAAC ALFARAFNQL
AKADVWEQTF WDSDKKEEIL TYMIRFPNSG FKIQALSSRP SNLRGLQGDV VIDEAAFHEA
LDELLKAAFA LNMWGASVRI ISTHNGVDNL FNQYIQDARE GRKDYSVHRI TLDDAIADGL
YRRICYVTNQ PWSPEAEKAW RDGLYRNAPN KESADEEYGC IPKKSGGAYL SRVLIEAAMT
PARDIPVLRF EAPDDFESLT PQMRHGIVQD WCEQELLPLL DALSPLNKHV LGEDFARRGD
LTVFVPLAIT PDLRKRECFR VELRNVTYDQ QRQILLFILS RLPRFTGAAF DATGNGGYLA
EAARLIYGPE MIDCISLTPA WYQEWMPKLK GEFEAQNITI ARHQTTLDDL LHIKVDKGIP
QIDKGRTKDE GGKGRRHGDF AVALCMAVRA SYMNGFVIDE DSIQALPPRH RGDDVDNDDF
DDYHQFERGG W