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Protein

Terminase, large subunit gp2

Gene

2

Organism
Bacillus phage SPP1 (Bacteriophage SPP1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 to initiate and to end a packaging reaction (PubMed:10930407). 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. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by the adapter (gp15) and the stopper protein (gp16) that form the connector.1 Publication2 Publications

Cofactori

Mn2+1 Publication, Mg2+1 PublicationNote: Binds 2 divalent metal cations per subunit. Optimum concentration of Mg2+ is 10 mm (PubMed:10930407). As the Mn2+ dose increases, gp2 converts supercoiled circular plasmid DNA to nicked open circular DNA, subsequently to linear DNA and finally to completely degraded DNA (PubMed:19444313).2 Publications

pH dependencei

Optimum pH is 7.8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei135For ATPase activitySequence analysis1
Metal bindingi266Manganese or magnesium 1; catalytic; for nuclease activityCombined sources1 Publication1
Metal bindingi266Manganese or magnesium 2; catalytic; for nuclease activity1 Publication1
Metal bindingi321Manganese or magnesium 1; catalytic; for nuclease activityCombined sources1 Publication1
Metal bindingi400Manganese or magnesium 2; catalytic; for nuclease activity1 Publication1

GO - Molecular functioni

  • endonuclease activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • nuclease activity Source: UniProtKB

GO - Biological processi

  • DNA packaging Source: InterPro
  • viral DNA genome packaging Source: UniProtKB

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processViral genome packaging, Viral release from host cell
LigandMagnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Terminase, large subunit gp2 (EC:3.1.-.-2 Publications)
Alternative name(s):
DNA-packaging protein G2P
Gene product 2
Short name:
gp2
Gene namesi
Name:2
OrganismiBacillus phage SPP1 (Bacteriophage SPP1)
Taxonomic identifieri10724 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdavirusunclassified Lambda-like viruses
Virus hostiBacillus subtilis [TaxID: 1423]
Proteomesi
  • UP000002559 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • viral terminase, large subunit Source: UniProtKB

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi266D → N: Complete loss of endonuclease activity. 1
Mutagenesisi321D → N: Complete loss of endonuclease activity. 1
Mutagenesisi400H → A: Decreased endonuclease activity. 1
Mutagenesisi403D → N: Complete loss of endonuclease activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000777891 – 422Terminase, large subunit gp2Add BLAST422

Interactioni

Subunit structurei

Monomer. Interacts with the terminase small subunit gp1; the active complex is probably heterooligomeric.1 Publication

Structurei

Secondary structure

1422
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi243 – 245Combined sources3
Helixi252 – 257Combined sources6
Beta strandi261 – 266Combined sources6
Beta strandi274 – 282Combined sources9
Turni283 – 286Combined sources4
Beta strandi287 – 298Combined sources12
Helixi301 – 310Combined sources10
Beta strandi318 – 320Combined sources3
Helixi325 – 333Combined sources9
Beta strandi340 – 342Combined sources3
Helixi347 – 349Combined sources3
Helixi350 – 358Combined sources9
Beta strandi360 – 365Combined sources6
Turni367 – 369Combined sources3
Helixi371 – 379Combined sources9
Beta strandi382 – 384Combined sources3
Beta strandi386 – 388Combined sources3
Beta strandi390 – 394Combined sources5
Beta strandi396 – 398Combined sources3
Helixi400 – 408Combined sources9
Helixi410 – 412Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WBNX-ray1.90A232-422[»]
2WC9X-ray2.50A232-422[»]
SMRiP54308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54308.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 198ATPase activityAdd BLAST198
Regioni232 – 422Nuclease activityAdd BLAST191

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi33 – 40Walker A motif8
Motifi130 – 135Walker B motif6

Phylogenomic databases

OrthoDBiVOG090000OD.

Family and domain databases

InterProiView protein in InterPro
IPR006437. Phage_terminase_lsu.
IPR035413. Terminase_L_C.
IPR035412. Terminase_L_N.
PfamiView protein in Pfam
PF04466. Terminase_3. 1 hit.
PF17288. Terminase_3C. 1 hit.
TIGRFAMsiTIGR01547. phage_term_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P54308-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVRLSEKF TPHFLEVWRT VKAAQHLKYV LKGGRGSAKS THIAMWIILL
60 70 80 90 100
MMMMPITFLV IRRVYNTVEQ SVFEQLKEAI DMLEVGHLWK VSKSPLRLTY
110 120 130 140 150
IPRGNSIIFR GGDDVQKIKS IKASKFPVAG MWIEELAEFK TEEEVSVIEK
160 170 180 190 200
SVLRAELPPG CRYIFFYSYN PPKRKQSWVN KVFNSSFLPA NTFVDHSTYL
210 220 230 240 250
QNPFLSKAFI EEAEEVKRRN ELKYRHEYLG EALGSGVVPF ENLQIEEGII
260 270 280 290 300
TDAEVARFDN IRQGLDFGYG PDPLAFVRWH YDKRKNRIYA IDELVDHKVS
310 320 330 340 350
LKRTADFVRK NKYESARIIA DSSEPRSIDA LKLEHGINRI EGAKKGPDSV
360 370 380 390 400
EHGERWLDEL DAIVIDPLRT PNIAREFENI DYQTDKNGDP IPRLEDKDNH
410 420
TIDATRYAFE RDMKKGGVSL WG
Length:422
Mass (Da):48,841
Last modified:October 1, 1996 - v1
Checksum:i55D16BDB32239A5C
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti18W → R in isolate Ts6M; temperature-sensitive. 1
Natural varianti73F → L in isolate SUS19. 1
Natural varianti233L → F in isolate SUS19. 1
Natural varianti412D → N in isolate Ts10M; temperature-sensitive. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56064 Genomic DNA. Translation: CAA39537.1.
X97918 Genomic DNA. Translation: CAA66573.1.
PIRiS24451.
RefSeqiNP_690654.1. NC_004166.2.

Genome annotation databases

GeneIDi955254.
KEGGivg:955254.

Similar proteinsi

Entry informationi

Entry nameiTERL_BPSPP
AccessioniPrimary (citable) accession number: P54308
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 22, 2017
This is version 85 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references