ID   HCP_LAMBD               Reviewed;          68 AA.
AC   P68660; P03727;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-SEP-2021, entry version 73.
DE   RecName: Full=Head completion protein;
DE            Short=HCP;
DE   AltName: Full=Head-tail joining protein W {ECO:0000305};
DE            Short=gpW;
GN   Name=W; OrderedLocusNames=lambdap03;
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, AND SUBUNIT.
RX   PubMed=5022189; DOI=10.1016/0022-2836(72)90082-4;
RA   Casjens S., Horn T., Kaiser A.D.;
RT   "Head assembly steps controlled by genes F and W in bacteriophage lambda.";
RL   J. Mol. Biol. 64:551-563(1972).
RN   [3]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14569303; DOI=10.1139/o03-059;
RA   Murialdo H., Xing X., Tzamtzis D., Haddad A., Gold M.;
RT   "The product of the bacteriophage lambda W gene: purification and
RT   properties.";
RL   Biochem. Cell Biol. 81:307-315(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=20660769; DOI=10.1073/pnas.1005822107;
RA   Cardarelli L., Pell L.G., Neudecker P., Pirani N., Liu A., Baker L.A.,
RA   Rubinstein J.L., Maxwell K.L., Davidson A.R.;
RT   "Phages have adapted the same protein fold to fulfill multiple functions in
RT   virion assembly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:14384-14389(2010).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=11302702; DOI=10.1006/jmbi.2001.4582;
RA   Maxwell K.L., Yee A.A., Booth V., Arrowsmith C.H., Gold M., Davidson A.R.;
RT   "The solution structure of bacteriophage lambda protein W, a small
RT   morphogenetic protein possessing a novel fold.";
RL   J. Mol. Biol. 308:9-14(2001).
RN   [6]
RP   STRUCTURE BY NMR OF 1-62.
RX   PubMed=22087227; DOI=10.1371/journal.pone.0026409;
RA   Sborgi L., Verma A., Munoz V., de Alba E.;
RT   "Revisiting the NMR structure of the ultrafast downhill folding protein gpW
RT   from bacteriophage lambda.";
RL   PLoS ONE 6:E26409-E26409(2011).
CC   -!- FUNCTION: Plays a role in morphogenesis of the virion head after genome
CC       packaging. Presumably interacts with the portal vertex to stabilize the
CC       packaged DNA within the head after packaging. Probably binds to the
CC       head-tail connector protein FII. {ECO:0000269|PubMed:14569303,
CC       ECO:0000269|PubMed:20660769, ECO:0000269|PubMed:5022189}.
CC   -!- SUBUNIT: Monomer in solution, assembles into hexamers on the prohead.
CC       May bind FII and portal protein (Potential). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:14569303}.
CC       Note=Probably part of the head-tail connector.
CC       {ECO:0000269|PubMed:20660769}.
CC   -!- SIMILARITY: Belongs to the lambda phage gpW family. {ECO:0000305}.
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DR   EMBL; J02459; AAA96535.1; -; Genomic_DNA.
DR   PIR; H43008; JQBPL.
DR   RefSeq; NP_040582.1; NC_001416.1.
DR   PDB; 1HYW; NMR; -; A=1-68.
DR   PDB; 2L6Q; NMR; -; A=1-62.
DR   PDB; 2L6R; NMR; -; A=1-62.
DR   PDBsum; 1HYW; -.
DR   PDBsum; 2L6Q; -.
DR   PDBsum; 2L6R; -.
DR   BMRB; P68660; -.
DR   SMR; P68660; -.
DR   IntAct; P68660; 1.
DR   GeneID; 2703525; -.
DR   KEGG; vg:2703525; -.
DR   EvolutionaryTrace; P68660; -.
DR   Proteomes; UP000001711; Genome.
DR   GO; GO:0019058; P:viral life cycle; IEA:InterPro.
DR   Gene3D; 3.30.1580.10; -; 1.
DR   InterPro; IPR004174; GpW.
DR   InterPro; IPR036626; GpW_sf.
DR   Pfam; PF02831; gpW; 1.
DR   SUPFAM; SSF64210; SSF64210; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Late protein; Reference proteome; Viral capsid assembly;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..68
FT                   /note="Head completion protein"
FT                   /id="PRO_0000077646"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:1HYW"
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:1HYW"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:1HYW"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:1HYW"
FT   HELIX           40..53
FT                   /evidence="ECO:0007829|PDB:1HYW"
FT   TURN            54..57
FT                   /evidence="ECO:0007829|PDB:1HYW"
SQ   SEQUENCE   68 AA;  7613 MW;  AD8A1788A7835F3A CRC64;
     MTRQEELAAA RAALHDLMTG KRVATVQKDG RRVEFTATSV SDLKKYIAEL EVQTGMTQRR
     RGPAGFYV