ID   DARA_BPP1               Reviewed;         639 AA.
AC   O21970;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Defense against restriction protein A {ECO:0000303|PubMed:3029954};
DE            Short=DarA;
GN   Name=darA;
OS   Escherichia phage P1 (Bacteriophage P1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Punavirus.
OX   NCBI_TaxID=2886926;
OH   NCBI_TaxID=543; Enterobacteriaceae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9813202; DOI=10.1006/viro.1998.9405;
RA   Iida S., Hiestand-Nauer R., Sandmeier H., Lehnherr H., Arber W.;
RT   "Accessory genes in the darA operon of bacteriophage P1 affect
RT   antirestriction function, generalized transduction, head morphogenesis, and
RT   host cell lysis.";
RL   Virology 251:49-58(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Mod1902::IS5 c1.100 rev dmt, and Mod749::IS5 c1.100 mutant;
RX   PubMed=15489417; DOI=10.1128/jb.186.21.7032-7068.2004;
RA   Lobocka M.B., Rose D.J., Plunkett G. III, Rusin M., Samojedny A.,
RA   Lehnherr H., Yarmolinsky M.B., Blattner F.R.;
RT   "Genome of bacteriophage P1.";
RL   J. Bacteriol. 186:7032-7068(2004).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=3029954; DOI=10.1016/0042-6822(87)90324-2;
RA   Iida S., Streiff M.B., Bickle T.A., Arber W.;
RT   "Two DNA antirestriction systems of bacteriophage P1, darA, and darB:
RT   characterization of darA- phages.";
RL   Virology 157:156-166(1987).
RN   [4]
RP   INDUCTION, PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=3029955; DOI=10.1016/0042-6822(87)90325-4;
RA   Streiff M.B., Iida S., Bickle T.A.;
RT   "Expression and proteolytic processing of the darA antirestriction gene
RT   product of bacteriophage P1.";
RL   Virology 157:167-171(1987).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=28509398; DOI=10.1111/mmi.13705;
RA   Piya D., Vara L., Russell W.K., Young R., Gill J.J.;
RT   "The multicomponent antirestriction system of phage P1 is linked to capsid
RT   morphogenesis.";
RL   Mol. Microbiol. 105:399-412(2017).
CC   -!- FUNCTION: Internal capsid protein that is probably ejected along with
CC       the viral DNA and prevents degradation of viral DNA by the host type I
CC       restriction-modification antiviral defense system (PubMed:3029954).
CC       Plays a role in directing proper capsid assembly (PubMed:28509398).
CC       {ECO:0000269|PubMed:28509398, ECO:0000269|PubMed:3029954}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:28509398,
CC       ECO:0000269|PubMed:3029955}. Note=Internal capsid protein. A
CC       proteolytically cleaved 60 kDa form is incorporated into the virion.
CC       {ECO:0000269|PubMed:3029954}.
CC   -!- INDUCTION: Expressed late in the viral replication cycle.
CC       {ECO:0000269|PubMed:3029955}.
CC   -!- PTM: Proteolytically cleaved into a 60 kDa form which is incorporated
CC       into the virion. {ECO:0000269|PubMed:3029955}.
CC   -!- MISCELLANEOUS: Phage P1 Dar antirestriction system is composed of Hdf,
CC       DarA, DdrA, DdrB, DarB and Ulx. Hdf and DarA are incorporated first in
CC       the procapsid in a co-dependent manner, followed by DarB, DdrB and Ulx.
CC       {ECO:0000269|PubMed:28509398}.
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DR   EMBL; AJ000741; CAA04283.1; -; Genomic_DNA.
DR   EMBL; AF234172; AAQ13998.1; -; Genomic_DNA.
DR   EMBL; AF234173; AAQ14106.1; -; Genomic_DNA.
DR   RefSeq; YP_006494.1; NC_005856.1.
DR   SMR; O21970; -.
DR   GeneID; 2777415; -.
DR   KEGG; vg:2777415; -.
DR   Proteomes; UP000001577; Genome.
DR   Proteomes; UP000008091; Genome.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0099018; P:evasion by virus of host restriction-modification system; IDA:UniProtKB.
DR   GO; GO:0019069; P:viral capsid assembly; IDA:UniProtKB.
DR   InterPro; IPR041501; DarA_C.
DR   InterPro; IPR041140; DarA_N.
DR   Pfam; PF18789; DarA_C; 1.
DR   Pfam; PF18788; DarA_N; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Coiled coil; Host-virus interaction; Late protein;
KW   Reference proteome; Restriction-modification system evasion by virus;
KW   Viral capsid assembly; Viral release from host cell; Virion.
FT   CHAIN           1..639
FT                   /note="Defense against restriction protein A"
FT                   /id="PRO_0000433212"
FT   REGION          382..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          201..284
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  69480 MW;  61F597D16F602CBC CRC64;
     MEQFNINKGM TIKPGLDVLP PPVTDDEYRA LMAGEDRYLM TESNTLEEIE ATFFYDTPIH
     WCATDLLEAI SSTRLQLHRT MQAFVRALNQ KLNGTGISAG SDKTGDVAQS GARAIGGAEI
     GRARNVNGLP VLPAIIPLSD GQTISILFHS PTAENRITNS DTLVAFQFLL NKKDVTHTVA
     PMSGRDMTLA QVTMKLANLA EKNSAKFQRA QKKKKALVDE ITQLQADSDQ KEDAMSDLAD
     QVAAVEGQKA DLEQKINAVA SEADSLYEEN ERLQGEIDRL NRTGGRDTIA PAGMTGGHSR
     ALTDRLASIK NRMHMDGEAT LSNGASMKQF IGDGEGYIQL TDPDGSVYMI KAKSIQGVDM
     ADAIGKLFKA YKAGNVSEYL VQPEEHKPEN VEPESAEDTG SSSPEPEVSV GAYRYALQMR
     PAAPGAIPEG NKAILPRPDE GDPYYEYARY GIATYDTPLS DQQMSEYDLK LLPREDSFDF
     LAKTLTNGPF GKYAQKALEL ATNSPDEFRV MLKTQFQKTF PNIAFPGGAG TEKMVQSMIN
     ALQAEVGEIT QPEPAPAQPD ETVSEADAEA NKAIEYLNNV MDMQSTDMAE IRNARGNVRE
     AIAALQTAGR FEENEELVNG AARHLADLLV AIQKAGVAA