DECO_LAMBD
ID DECO_LAMBD Reviewed; 110 AA.
AC P03712;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Capsid decoration protein;
DE AltName: Full=Auxiliary protein D;
DE AltName: Full=Gene product D;
DE Short=gpD;
DE AltName: Full=Major capsid protein D;
GN Name=D; OrderedLocusNames=lambdap07;
OS Escherichia phage lambda (Bacteriophage lambda).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage lambda DNA.";
RL J. Mol. Biol. 162:729-773(1982).
RN [2]
RP FUNCTION, SUBUNIT, TRIMERIZATION, AND INTERACTION WITH MAJOR CAPSID
RP PROTEIN.
RX PubMed=8411174; DOI=10.1006/jmbi.1993.1545;
RA Dokland T., Murialdo H.;
RT "Structural transitions during maturation of bacteriophage lambda
RT capsids.";
RL J. Mol. Biol. 233:682-694(1993).
RN [3]
RP FUNCTION.
RX PubMed=18786402; DOI=10.1016/j.str.2008.05.016;
RA Lander G.C., Evilevitch A., Jeembaeva M., Potter C.S., Carragher B.,
RA Johnson J.E.;
RT "Bacteriophage lambda stabilization by auxiliary protein gpD: timing,
RT location, and mechanism of attachment determined by cryo-EM.";
RL Structure 16:1399-1406(2008).
RN [4]
RP FUNCTION, PROTEIN DISORDER, AND INTERACTION WITH MAJOR CAPSID PROTEIN.
RX PubMed=21821043; DOI=10.1016/j.jmb.2011.07.045;
RA Medina E.M., Andrews B.T., Nakatani E., Catalano C.E.;
RT "The bacteriophage lambda gpNu3 scaffolding protein is an intrinsically
RT disordered and biologically functional procapsid assembly catalyst.";
RL J. Mol. Biol. 412:723-736(2011).
RN [5]
RP PROTEIN SEQUENCE.
RX PubMed=6233140; DOI=10.1002/j.1460-2075.1982.tb01355.x;
RA Witkiewicz H., Schweiger M.;
RT "The head protein D of bacterial virus lambda is related to eukaryotic
RT chromosomal proteins.";
RL EMBO J. 1:1559-1564(1982).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 16-110.
RX PubMed=10700283; DOI=10.1038/73347;
RA Yang F., Forrer P., Dauter Z., Conway J.F., Cheng N., Cerritelli M.E.,
RA Steven A.C., Pluckthun A., Wlodawer A.;
RT "Novel fold and capsid-binding properties of the lambda-phage display
RT platform protein gpD.";
RL Nat. Struct. Biol. 7:230-237(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 16-110.
RX PubMed=15317025; DOI=10.1002/prot.20254;
RA Chang C., Pluckthun A., Wlodawer A.;
RT "Crystal structure of a truncated version of the phage lambda protein
RT gpD.";
RL Proteins 57:866-868(2004).
RN [8]
RP STRUCTURE BY NMR OF 2-110.
RX PubMed=15929002; DOI=10.1007/s10858-005-0945-7;
RA Iwai H., Forrer P., Pluckthun A., Guntert P.;
RT "NMR solution structure of the monomeric form of the bacteriophage lambda
RT capsid stabilizing protein gpD.";
RL J. Biomol. NMR 31:351-356(2005).
CC -!- FUNCTION: Stabilizes the expansion of the capsid head shell after
CC genome packaging. The packaging of viral genome in the procapsid
CC triggers a dramatic reconfiguration of the capsid shell, expanding from
CC roughly 50nm to 60nm while the capsid thickness decreases. 415 capsid
CC decoration protein molecules cooperatively bind the expanded capsid,
CC thereby stabilizing the mature capsid shell.
CC {ECO:0000269|PubMed:18786402, ECO:0000269|PubMed:21821043,
CC ECO:0000269|PubMed:8411174}.
CC -!- SUBUNIT: Homotrimer. Interacts with major capsid protein.
CC {ECO:0000269|PubMed:21821043, ECO:0000269|PubMed:8411174}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm.
CC -!- SIMILARITY: Belongs to the lambda phage gpD family. {ECO:0000305}.
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DR EMBL; J02459; AAA96539.1; -; Genomic_DNA.
DR PIR; G04333; VHBPDL.
DR RefSeq; NP_040586.1; NC_001416.1.
DR PDB; 1C5E; X-ray; 1.10 A; A/B/C=16-110.
DR PDB; 1TCZ; X-ray; 1.85 A; A/B/C/D/E/F=16-110.
DR PDB; 1VD0; NMR; -; A=2-110.
DR PDB; 5MFD; X-ray; 2.30 A; B/D/F/H=21-110.
DR PDB; 7VII; EM; 5.60 A; H/I/J/K/L/M/N=1-110.
DR PDB; 7VIK; EM; 3.76 A; H/I/J/K/L/M/N=1-110.
DR PDBsum; 1C5E; -.
DR PDBsum; 1TCZ; -.
DR PDBsum; 1VD0; -.
DR PDBsum; 5MFD; -.
DR PDBsum; 7VII; -.
DR PDBsum; 7VIK; -.
DR BMRB; P03712; -.
DR SMR; P03712; -.
DR IntAct; P03712; 1.
DR GeneID; 2703529; -.
DR KEGG; vg:2703529; -.
DR EvolutionaryTrace; P03712; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098021; C:viral capsid, decoration; IDA:UniProtKB.
DR GO; GO:0019073; P:viral DNA genome packaging; IDA:CACAO.
DR InterPro; IPR004195; Head_decoration_D.
DR InterPro; IPR036630; Head_decoration_D_sf.
DR Pfam; PF02924; HDPD; 1.
DR SUPFAM; SSF51274; SSF51274; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid decoration protein; Capsid protein;
KW Direct protein sequencing; Host cytoplasm; Late protein;
KW Reference proteome; Viral capsid assembly; Viral release from host cell;
KW Virion.
FT CHAIN 1..110
FT /note="Capsid decoration protein"
FT /id="PRO_0000077597"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1C5E"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1C5E"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1C5E"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1C5E"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:5MFD"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1C5E"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1C5E"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1C5E"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1C5E"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:1C5E"
FT TURN 100..104
FT /evidence="ECO:0007829|PDB:1C5E"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1C5E"
SQ SEQUENCE 110 AA; 11572 MW; F8552FBA2B107801 CRC64;
MTSKETFTHY QPQGNSDPAH TATAPGGLSA KAPAMTPLML DTSSRKLVAW DGTTDGAAVG
ILAVAADQTS TTLTFYKSGT FRYEDVLWPE AASDETKKRT AFAGTAISIV
