CAPSD_LAMBD
ID CAPSD_LAMBD Reviewed; 341 AA.
AC P03713;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Major capsid protein {ECO:0000255|HAMAP-Rule:MF_04133, ECO:0000303|PubMed:265585};
DE AltName: Full=Gene product E {ECO:0000255|HAMAP-Rule:MF_04133};
DE Short=gpE {ECO:0000255|HAMAP-Rule:MF_04133};
DE AltName: Full=Major head protein {ECO:0000255|HAMAP-Rule:MF_04133};
GN Name=E {ECO:0000255|HAMAP-Rule:MF_04133}; OrderedLocusNames=lambdap08;
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, AND SUBCELLULAR LOCATION.
RX PubMed=265585; DOI=10.1073/pnas.74.3.906;
RA Murialdo H., Becker A.;
RT "Assembly of biologically active proheads of bacteriophage lambda in
RT vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:906-910(1977).
RN [3]
RP FUNCTION.
RX PubMed=2141087; DOI=10.1016/s0022-2836(05)80211-6;
RA Katsura I., Kobayashi H.;
RT "Structure and inherent properties of the bacteriophage lambda head shell.
RT VII. Molecular design of the form-determining major capsid protein.";
RL J. Mol. Biol. 213:503-511(1990).
RN [4]
RP FUNCTION, AND SUBUNIT.
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 [5]
RP CAUTION.
RX PubMed=20620152; DOI=10.1016/j.jmb.2010.06.060;
RA Medina E., Wieczorek D., Medina E.M., Yang Q., Feiss M., Catalano C.E.;
RT "Assembly and maturation of the bacteriophage lambda procapsid: gpC is the
RT viral protease.";
RL J. Mol. Biol. 401:813-830(2010).
RN [6]
RP INTERACTION WITH F1 PROTEIN.
RX PubMed=22801427; DOI=10.1074/jbc.m112.378349;
RA Popovic A., Wu B., Arrowsmith C.H., Edwards A.M., Davidson A.R.,
RA Maxwell K.L.;
RT "Structural and biochemical characterization of phage lambda FI protein
RT (gpFI) reveals a novel mechanism of DNA packaging chaperone activity.";
RL J. Biol. Chem. 287:32085-32095(2012).
CC -!- FUNCTION: Assembles to form an icosahedral capsid with a T=7 symmetry.
CC The icosahedral capsid is about 60 nm in diameter and composed of 415
CC major capsid proteins. The assembly is primed by the interaction
CC between capsid assembly protease and portal dodecamer, and major capsid
CC proteins assemble cooperatively to form the procapsid with the help of
CC capsid scaffolding protein. Major capsid protein forms hexons and
CC pentons of the icosahedron. Viral genomic DNA is packaged into the
CC procapsid through the portal vertex (By similarity). The packaging
CC triggers a dramatic reconfiguration of the capsid shell, expanding from
CC roughly 50nm to 60nm while the capsid thickness decreases. The capsid
CC decoration protein binds the expanded capsid and stabilizes it.
CC {ECO:0000255|HAMAP-Rule:MF_04133, ECO:0000269|PubMed:2141087,
CC ECO:0000269|PubMed:265585, ECO:0000269|PubMed:8411174}.
CC -!- SUBUNIT: Homomultimer (PubMed:265585, PubMed:8411174). Interacts with
CC FI protein (PubMed:22801427). {ECO:0000269|PubMed:22801427,
CC ECO:0000269|PubMed:265585, ECO:0000269|PubMed:8411174}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04133,
CC ECO:0000269|PubMed:265585}. Host cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_04133, ECO:0000269|PubMed:265585}. Note=Forms the capsid
CC icosahedric shell. {ECO:0000255|HAMAP-Rule:MF_04133,
CC ECO:0000269|PubMed:265585}.
CC -!- SIMILARITY: Belongs to the lambda phage major capsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04133}.
CC -!- CAUTION: Some of the E protein may be covalently linked with an
CC equimolar amount of protein C and cleaved to yield minor capsid
CC proteins X1 and X2. But recent data fail to detect cleavage products.
CC {ECO:0000305}.
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DR EMBL; J02459; AAA96540.1; -; Genomic_DNA.
DR PIR; H04333; VHBPEL.
DR RefSeq; NP_040587.1; NC_001416.1.
DR PDB; 7VI9; EM; 5.03 A; A/B/C/D/E/F/G=1-341.
DR PDB; 7VIA; EM; 3.88 A; A/B/C/D/E/F/G=1-341.
DR PDB; 7VII; EM; 5.60 A; A/B/C/D/E/F/G=1-341.
DR PDB; 7VIK; EM; 3.76 A; A/B/C/D/E/F/G=1-341.
DR PDBsum; 7VI9; -.
DR PDBsum; 7VIA; -.
DR PDBsum; 7VII; -.
DR PDBsum; 7VIK; -.
DR SMR; P03713; -.
DR IntAct; P03713; 3.
DR PRIDE; P03713; -.
DR GeneID; 2703482; -.
DR KEGG; vg:2703482; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR HAMAP; MF_04133; CAPSID_LAMBDA; 1.
DR InterPro; IPR005564; Major_capsid_GpE.
DR Pfam; PF03864; Phage_cap_E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host cytoplasm; Late protein;
KW Reference proteome; T=7 icosahedral capsid protein; Virion.
FT CHAIN 1..341
FT /note="Major capsid protein"
FT /id="PRO_0000077565"
SQ SEQUENCE 341 AA; 38188 MW; 31C50E4B38DA44A9 CRC64;
MSMYTTAQLL AANEQKFKFD PLFLRLFFRE SYPFTTEKVY LSQIPGLVNM ALYVSPIVSG
EVIRSRGGST SEFTPGYVKP KHEVNPQMTL RRLPDEDPQN LADPAYRRRR IIMQNMRDEE
LAIAQVEEMQ AVSAVLKGKY TMTGEAFDPV EVDMGRSEEN NITQSGGTEW SKRDKSTYDP
TDDIEAYALN ASGVVNIIVF DPKGWALFRS FKAVKEKLDT RRGSNSELET AVKDLGKAVS
YKGMYGDVAI VVYSGQYVEN GVKKNFLPDN TMVLGNTQAR GLRTYGCIQD ADAQREGINA
SARYPKNWVT TGDPAREFTM IQSAPLMLLA DPDEFVSVQL A
