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Q9T1V4 (BP45_BPMU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Baseplate puncturing device gp45
Alternative name(s):
Gene product 45
Short name=gp45
Gene product Q
Short name=gpQ
Gene names
Ordered Locus Names:Mup45
OrganismEnterobacteria phage Mu (Bacteriophage Mu) [Reference proteome]
Taxonomic identifier10677 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeMulikevirus
Virus hostEnterobacteriaceae [TaxID: 543]

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the baseplate that forms a central needlelike spike used to puncture the host cell membrane for tube insertion during virus entry. Probably involved in baseplate and tail assembly. Serves as the distal plug of tail tube channel and might regulate the process of the phage DNA and protein ejection into the host cell. Ref.4 Ref.6

Cofactor

Binds 1 calcium ion per trimer. Calcium ion plays an important role in interaction with the host cell membrane. Ref.6

Binds 1 chloride ion per trimer. Ref.6

Binds 1 iron ion per trimer. Ref.6

Subunit structure

Homotrimer. Ref.4 Ref.6

Subcellular location

Virion. Host cytoplasm Probable. Note: Baseplate Probable.

Induction

Expressed in the late phase of the viral replicative cycle. Expression of late genes is activated by the viral late transcription activator C. Ref.3

Domain

The C-terminus is a needlelike shaped homotrimer consisting of an intertwined beta-sheet, a triple beta-helix and a metal-binding region. Ref.6

Disruption phenotype

No tail is synthesized. Ref.2

Caution

Translation initiates from a non-canonical start codon (GUG).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Baseplate puncturing device gp45
PRO_0000077838

Regions

Region177 – 19721Ions binding

Sites

Metal binding1831Iron; via tele nitrogen; shared with trimeric partners
Metal binding1851Iron; via tele nitrogen; shared with trimeric partners
Metal binding1881Calcium; shared with trimeric partners
Metal binding1891Calcium; shared with trimeric partners
Binding site1881Chloride; via amide nitrogen; shared with trimeric partners

Experimental info

Mutagenesis1881D → A: Loss of membrane-binding ability. Ref.6

Secondary structure

..................... 197
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9T1V4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 448C7A7ADCADD5C9

FASTA19721,689
        10         20         30         40         50         60 
MERVNDSALN RLLTPLMRRV RLMLARAVVN VINDGRKVQN LQVGLLDDEE SDEVERLQNY 

        70         80         90        100        110        120 
GHFSVPLPGA EALIACVGAQ RDQGIAVVVE DRRYRPTNLE PGDAGIYHHE GHRIRLTKDG 

       130        140        150        160        170        180 
RCIITCKTVE VYADESMTVD TPRTTFTGDV EIQKGLGVKG KSQFDSNITA PDAIINGKST 

       190 
DKHIHRGDSG GTTGPMQ 

« Hide

References

« Hide 'large scale' references
[1]"Bacteriophage Mu genome sequence: analysis and comparison with Mu-like prophages in Haemophilus, Neisseria and Deinococcus."
Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.
J. Mol. Biol. 317:337-359(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Morphogenetic structures present in lysates of amber mutants of bacteriophage Mu."
Grundy F.J., Howe M.M.
Virology 143:485-504(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[3]"Mutational analysis of a C-dependent late promoter of bacteriophage Mu."
Chiang L.W., Howe M.M.
Genetics 135:619-629(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[4]"The C-terminal domain is sufficient for host-binding activity of the Mu phage tail-spike protein."
Suzuki H., Yamada S., Toyama Y., Takeda S.
Biochim. Biophys. Acta 1804:1738-1742(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[5]"Contractile tail machines of bacteriophages."
Leiman P.G., Shneider M.M.
Adv. Exp. Med. Biol. 726:93-114(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"Crystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ion."
Harada K., Yamashita E., Nakagawa A., Miyafusa T., Tsumoto K., Ueno T., Toyama Y., Takeda S.
Biochim. Biophys. Acta 1834:284-291(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 92-197, FUNCTION, SUBUNIT, DOMAIN, COFACTOR, MUTAGENESIS OF ASP-188.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083977 Genomic DNA. Translation: AAF01123.1.
RefSeqNP_050649.1. NC_000929.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VTNX-ray1.75A100-197[»]
3VTOX-ray1.44A/B/C/P/Q/R92-197[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2636280.

Family and domain databases

InterProIPR013046. Phage_Mu/P2_baseplate_assem.
IPR014462. Phage_Mu_Gp45.
[Graphical view]
PfamPF06890. Phage_Mu_Gp45. 1 hit.
[Graphical view]
PIRSFPIRSF012337. gp45. 1 hit.
TIGRFAMsTIGR01644. phage_P2_V. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBP45_BPMU
AccessionPrimary (citable) accession number: Q9T1V4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references