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Protein

Terminase, large subunit gp19

Gene

19

Organism
Enterobacteria phage T7 (Bacteriophage T7)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome at a unique and precise dsDNA sequence to initiate and to end a packaging reaction (By similarity). The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities (By similarity). Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine (By similarity). The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer (By similarity). Once the DNA is packaged, the terminase detaches from the connector and gets replaced by the tail to finish maturation of the virion (PubMed:23632014).By similarity1 Publication

Cofactori

Mg2+By similarityNote: Binds 2 Mg2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi364Magnesium 1; catalytic; for nuclease activityBy similarity1
Metal bindingi364Magnesium 2; catalytic; for nuclease activityBy similarity1
Metal bindingi420Magnesium 2; catalytic; for nuclease activityBy similarity1
Metal bindingi518Magnesium 1; catalytic; for nuclease activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi58 – 65ATPSequence analysis8

GO - Molecular functioni

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processViral genome packaging, Viral release from host cell
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Terminase, large subunit gp19 (EC:3.1.-.-By similarity)
Alternative name(s):
DNA-packaging protein B
Gene product 19
Short name:
Gp19
Gene namesi
Ordered Locus Names:19
OrganismiEnterobacteria phage T7 (Bacteriophage T7)
Taxonomic identifieri10760 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7virus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000000840 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001065411 – 586Terminase, large subunit gp19Add BLAST586

Proteomic databases

PRIDEiP03694

Interactioni

Subunit structurei

Homopentamer. Interacts with the terminase small subunit gp19; the active complex is probably heterooligomeric. Interacts with the head-to-tail connector protein gp8.1 Publication

Protein-protein interaction databases

IntActiP03694, 1 interactor
MINTiP03694

Structurei

3D structure databases

SMRiP03694
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 229ATPase activity1 PublicationAdd BLAST229
Regioni344 – 429Nuclease activity1 PublicationAdd BLAST86

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi58 – 65Walker A motifBy similarity8
Motifi156 – 161Walker B motifBy similarity6

Sequence similaritiesi

Belongs to the T7likevirus large terminase family.Curated

Phylogenomic databases

OrthoDBiVOG090000E5

Sequencei

Sequence statusi: Complete.

P03694-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTQSNRNAL VVAQLKGDFV AFLFVLWKAL NLPVPTKCQI DMAKVLANGD
60 70 80 90 100
NKKFILQAFR GIGKSFITCA FVVWSLWRDP QLKILIVSAS KERADANSIF
110 120 130 140 150
IKNIIDLLPF LSELKPRPGQ RDSVISFDVG PANPDHSPSV KSVGITGQLT
160 170 180 190 200
GSRADIIIAD DVEIPSNSAT MGAREKLWTL VQEFAALLKP LPSSRVIYLG
210 220 230 240 250
TPQTEMTLYK ELEDNRGYTT IIWPALYPRT REENLYYSQR LAPMLRAEYD
260 270 280 290 300
ENPEALAGTP TDPVRFDRDD LRERELEYGK AGFTLQFMLN PNLSDAEKYP
310 320 330 340 350
LRLRDAIVAA LDLEKAPMHY QWLPNRQNII EDLPNVGLKG DDLHTYHDCS
360 370 380 390 400
NNSGQYQQKI LVIDPSGRGK DETGYAVLYT LNGYIYLMEA GGFRDGYSDK
410 420 430 440 450
TLELLAKKAK QWGVQTVVYE SNFGDGMFGK VFSPILLKHH NCAMEEIRAR
460 470 480 490 500
GMKEMRICDT LEPVMQTHRL VIRDEVIRAD YQSARDVDGK HDVKYSLFYQ
510 520 530 540 550
MTRITREKGA LAHDDRLDAL ALGIEYLRES MQLDSVKVEG EVLADFLEEH
560 570 580
MMRPTVAATH IIEMSVGGVD VYSEDDEGYG TSFIEW
Length:586
Mass (Da):66,261
Last modified:July 21, 1986 - v1
Checksum:i0030B8EE701CB0A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01146 Genomic DNA Translation: CAA24440.1
PIRiS42338 JVBPB7
RefSeqiNP_042010.1, NC_001604.1

Genome annotation databases

GeneIDi1261062
KEGGivg:1261062

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01146 Genomic DNA Translation: CAA24440.1
PIRiS42338 JVBPB7
RefSeqiNP_042010.1, NC_001604.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BIJelectron microscopy16.00A/B/C/D/E1-476[»]
4BILelectron microscopy29.00A/B/C/D/E1-476[»]
SMRiP03694
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03694, 1 interactor
MINTiP03694

Proteomic databases

PRIDEiP03694

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1261062
KEGGivg:1261062

Phylogenomic databases

OrthoDBiVOG090000E5

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiTERL_BPT7
AccessioniPrimary (citable) accession number: P03694
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 23, 2018
This is version 72 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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