ID   SCAF_LAMBD              Reviewed;         439 AA.
AC   P03711;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Capsid assembly protease C;
DE            EC=3.4.21.-;
DE   AltName: Full=Gene product C;
DE            Short=GPC;
DE   AltName: Full=Minor capsid protein C;
GN   Name=C;
GN   and
GN   Name=NU3; OrderedLocusNames=lambdap05;
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 (ISOFORM CAPSID SCAFFOLDING PROTEIN NU3).
RX   PubMed=1090075; DOI=10.1016/0042-6822(75)90096-3;
RA   Ray P., Murialdo H.;
RT   "The role of gene Nu3 in bacteriophage lambda head morphogenesis.";
RL   Virology 64:247-263(1975).
RN   [3]
RP   CHARACTERIZATION (ISOFORM CAPSID SCAFFOLDING PROTEIN NU3).
RX   PubMed=1530932; DOI=10.1016/s0021-9258(18)48516-x;
RA   Ziegelhoffer T., Yau P., Chandrasekhar G.N., Kochan J., Georgopoulos C.,
RA   Murialdo H.;
RT   "The purification and properties of the scaffolding protein of
RT   bacteriophage lambda.";
RL   J. Biol. Chem. 267:455-461(1992).
RN   [4]
RP   FUNCTION, CAUTION (ISOFORM CAPSID ASSEMBLY PROTEASE C), AND MUTAGENESIS OF
RP   SER-166.
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   [5]
RP   FUNCTION OF CAPSID SCAFFOLDING PROTEIN NU3, AND INTERACTION WITH MAJOR
RP   CAPSID PROTEIN GPE (ISOFORM CAPSID SCAFFOLDING PROTEIN NU3).
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).
CC   -!- FUNCTION: Assembly protease promotes icosahedral procapsid assembly.
CC       Autocatalytic cleavage may release the capsid scaffolding protein. The
CC       protease domain catalyzes the cleavage of the capsid scaffolding
CC       protein after complete procapsid formation. Assembly protease and
CC       cleavages products are evicted from the capsid before or during DNA
CC       packaging.
CC   -!- FUNCTION: Scaffolding protein Nu3 promotes icosahedral procapsid
CC       assembly. Acts by binding the major capsid protein gpE and
CC       multimerizing in interaction with portal dodecamer, thereby placing gpE
CC       in a context facilitating icosahedral procapsid formation. Cleaved by
CC       capsid assembly protease C after capsid completion. The cleavages
CC       products are evicted from the capsid before or during DNA packaging.
CC   -!- SUBUNIT: Capsid assembly protease interacts with capsid scaffolding
CC       protein Nu3. Capsid scaffolding protein Nu3 multimerizes and interacts
CC       with major capsid protein gpE.
CC   -!- INTERACTION:
CC       P03711; P03711: NU3; NbExp=3; IntAct=EBI-4478358, EBI-4478358;
CC   -!- SUBCELLULAR LOCATION: [Isoform Capsid assembly protease C]: Virion.
CC       Host cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform Capsid scaffolding protein Nu3]: Host
CC       cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Capsid assembly protease C;
CC         IsoId=P03711-1; Sequence=Displayed;
CC       Name=Capsid scaffolding protein Nu3;
CC         IsoId=P03711-2; Sequence=VSP_054968;
CC   -!- MISCELLANEOUS: It is uncertain wether Val-260 or Met-309 is the
CC       initiator for Capsid scaffolding protein Nu3.
CC   -!- MISCELLANEOUS: [Isoform Capsid scaffolding protein Nu3]: Produced by
CC       alternative initiation at Met-309 of isoform. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S49 family. {ECO:0000305}.
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 cleavages products.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA96538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J02459; AAA96537.1; -; Genomic_DNA.
DR   EMBL; J02459; AAA96538.1; ALT_INIT; Genomic_DNA.
DR   PIR; A04333; VHBPCL.
DR   RefSeq; NP_040584.1; NC_001416.1. [P03711-1]
DR   RefSeq; NP_040585.1; NC_001416.1.
DR   SMR; P03711; -.
DR   IntAct; P03711; 4.
DR   MEROPS; S49.003; -.
DR   GeneID; 2703527; -.
DR   GeneID; 2703528; -.
DR   KEGG; vg:2703527; -.
DR   KEGG; vg:2703528; -.
DR   Proteomes; UP000001711; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW.
DR   CDD; cd07022; S49_Sppa_36K_type; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR033855; Protein_C.
DR   Pfam; PF01343; Peptidase_S49; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Capsid protein; Host cytoplasm; Hydrolase;
KW   Protease; Reference proteome; Serine protease; Viral capsid assembly;
KW   Viral capsid maturation; Viral release from host cell; Virion.
FT   CHAIN           1..439
FT                   /note="Capsid assembly protease C"
FT                   /id="PRO_0000027358"
FT   REGION          303..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..308
FT                   /note="Missing (in isoform Capsid scaffolding protein Nu3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054968"
FT   MUTAGEN         166
FT                   /note="S->A: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:20620152"
SQ   SEQUENCE   439 AA;  45940 MW;  355ED56D60F6CDDF CRC64;
     MTAELRNLPH IASMAFNEPL MLEPAYARVF FCALAGQLGI SSLTDAVSGD SLTAQEALAT
     LALSGDDDGP RQARSYQVMN GIAVLPVSGT LVSRTRALQP YSGMTGYNGI IARLQQAASD
     PMVDGILLDM DTPGGMVAGA FDCADIIARV RDIKPVWALA NDMNCSAGQL LASAASRRLV
     TQTARTGSIG VMMAHSNYGA ALEKQGVEIT LIYSGSHKVD GNPYSHLPDD VRETLQSRMD
     ATRQMFAQKV SAYTGLSVQV VLDTEAAVYS GQEAIDAGLA DELVNSTDAI TVMRDALDAR
     KSRLSGGRMT KETQSTTVSA TASQADVTDV VPATEGENAS AAQPDVNAQI TAAVAAENSR
     IMGILNCEEA HGREEQARVL AETPGMTVKT ARRILAAAPQ SAQARSDTAL DRLMQGAPAP
     LAAGNPASDA VNDLLNTPV