DARB_BPP1
ID DARB_BPP1 Reviewed; 2255 AA.
AC Q71TF8;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Defense against restriction protein B {ECO:0000303|PubMed:3029954};
DE EC=3.6.4.- {ECO:0000305};
DE AltName: Full=DarB {ECO:0000312|EMBL:AAQ14093.1};
GN Name=darB {ECO:0000312|EMBL:AAQ14093.1};
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].
RC STRAIN=Mod1902::IS5 c1.100 rev dmt {ECO:0000312|EMBL:AAQ14093.1}, and
RC 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 [2]
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 [3]
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: Capsid internal protein that is probably ejected along with
CC the viral DNA and prevents degradation of viral DNA by the host EcoB
CC and EcoK restriction-modification antiviral defense systems.
CC {ECO:0000269|PubMed:28509398, ECO:0000269|PubMed:3029954}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:28509398,
CC ECO:0000269|PubMed:3029954}. Note=Internal capsid protein. DarA is
CC required for DarB incorporation into the virions.
CC {ECO:0000269|PubMed:28509398}.
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}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; AF234172; AAQ13985.1; -; Genomic_DNA.
DR EMBL; AF234173; AAQ14093.1; -; Genomic_DNA.
DR RefSeq; YP_006479.1; NC_005856.1.
DR GeneID; 2777481; -.
DR KEGG; vg:2777481; -.
DR Proteomes; UP000001577; Genome.
DR Proteomes; UP000008091; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IMP:UniProtKB.
DR Gene3D; 3.40.50.10810; -; 2.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038718; SNF2-like_sf.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Helicase; Host-virus interaction; Hydrolase;
KW Nucleotide-binding; Reference proteome;
KW Restriction-modification system evasion by virus; Virion.
FT CHAIN 1..2255
FT /note="Defense against restriction protein B"
FT /id="PRO_0000433213"
FT DOMAIN 841..1126
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1383..1568
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT COILED 1198..1234
FT /evidence="ECO:0000255"
FT COILED 1617..1654
FT /evidence="ECO:0000255"
FT MOTIF 1052..1055
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 854..861
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 2255 AA; 251543 MW; 383BAA4D9D28341F CRC64;
MNKLSMGVFR CSSVSEILKY IRAITSHRAP IKYGVEKVEG KSYDRLRREA NQKAIDLLNS
LVDGATLTDE QRQILAGYTG EGGIGGSVSE YYTPKPIAEG VWEIMKLYGA DVGNTLEPSA
GTGVFNETKP VGTVMTATEI SSVSGRINQL LHPEDSVQIS PFEQLAVSTP NDSFDHVVGN
VPFGGRDNTR NIDKPYAEET DMGSYFMLRM LDKIKPGGFM CVIVPPSIVS GSNMKRLRLR
LSRKAEFLGA HRLPTGTFDA NGTSTVVDVV LMRKHPAEMA EKIPLVHEST LESANVLWPT
FISGKWFEKD GRRFVHGTQE KGFQGRIEVR ADGQIDNQAL KAKLIHCFES RIDWYLLDMA
EPSPTADVVD EGEMRLINGV WQKYAGGRWI ESDAGKELKI DVASYGADSW EALQRNLTTT
EGRLGMTFTQ MANVRDKYTT SISDDMVQLV DWINSQPEKY RERLYRGAMI GRMLIEYQDM
KAAGHSAEQI EQQRLSLVSR LQAEIDRFGN PGRGPIAKLS GSGARAWFAF RGAIKLDGTI
SDELTGKLVT HDSSASYDST SYQDTLRYLY SDLTRDPIQL DDFRLAFTGE LPASDDELLN
LLASTPGIAV SPYGGIVPFA RATSGDINEI VAPKQEFLAT LTDGPVKNNV LNQLAAIEEK
RIKTPAENIR FKLNSRWFDR SVILEFLQEN GYPDLRYVQS VQLEGDEMVS DTYHGGDGLF
VGHRYGVVQR KDKETGEIRY EWDRKSGENA TGFPAQLEKY LNGARIGGKD SATANGYREQ
MALLEDQFNK WIKTHDRYDE LVAKYNDVFN SNIPYEHSGD PLGLKGLSGK RQPFDYQNSE
VRRLSEDGRG ILGFGTGLGK TTTALALEAF NYENGRSTRT AYVVPKSVLE NWYYEAKEFL
SEEAFSNYLF VGLDVLMDGD QIRQVPVLDE NGKPVLGTDG TPVMRDALKL ADEATITARM
NAIPHSNYRA VVFTKEQYAR IPLRDDTVDE HAQDMLYDFV AAGRVASAMD SDSHRKEAAR
RRVLSEYSDT GTEKAEKYPY FEDMGFDSVI ADEGHNYRNS YKNGREASQL AYLPTSAVAQ
SARDMAIKNA YLMKKNGGRG PVLLTATPVV NTPIDAYNML SHVLPKEYWQ KMGIYGPDDF
VKFFGKTRLE TVQKISGEVE EKMALVGFEN LDALRGIFHR WTTLKTAEDV KDTVEIPELD
EHQQDAPLTE EQLAAYEELR QQAEAAAKAN NGVTTSVNED GVIEHEKARP IFSIIRDMDR
VCTDMDLYYR RITYRFLPEY ADAVQQLADS LPKQATSEDD DSDDSITQQS QYSLIDKGEF
IQLQVPEAFE QEVNKRLARF GIDEQTVTHP VTPKYAKLIA TLKEFFPEGK QIIFTDEKTQ
HQKLKRIICN ALNLEPSKVG ILNAQTVAEA GKTGKKLKAV KPPKELPDEP TDAQIAKYNE
QMALYDAYIA QQNEMSLGGL EKIAADFQEG RTPIIICNKK AEVGINLHRG TTDIHHLTLP
WTPASIAQRN GRGARVGSNR ASVRVHYYCG KGSFDEYRLK TLKRKAGWIS DILRSDKSEM
ENADANDMIE MQMYTAKDDG ERLAMMQVQM DKAKAAQRAR QKEQATIDLQ NYIKAQHAAG
EDVEVLTAEL ERSKAELEKT TAEVAKFKQA VMAKAADNAD WKARWGSVHH TDRMLLAQYR
ASLKSAIQRK ANISQAISPY EKLLNRTQKA ATDIKRLRPL VEDAINKGIL DVDPDLVNHA
SEFLVIGDRS WRVGQYYDCA GDIVRIKSLD FDSQRADVEI IFTFKGTKSG NWDVKTLDKQ
VDVTPDEDAV MQKISGGVSI AGINDIISCD DFYRFQQRGM IKITDSYGVQ TTESGYSIDF
VGTYTDPLKH AVYPDRRDGA LKSSIAKWVL GMMSEGNNRQ VRLAEVFLTE LFGSNYGDVI
ASYGDTLSPE AIQEKIADAI ARMPEKTSQG ATRNGDSELE VTNAIFGTHE FRASDYEITT
AQFGTIGIYS NKAEIKQAMD AASARIAAER EANLNHAVAA LTQSWVTAIR EAATTGKITP
AIADVVNDGS KFMDAYKMDA VQLPSAYGQL SYRMTYNLVS MFSDLAILGL VDLNEVTPEL
LSMRKNHVEI LQRINTVLAG RTDEEKQADA DRINLALGNI TEEEIAARNE KQEELSSIQG
DATSIAQSLG LNYRVSTADL KMMYAPKFAA GEVFGLQEAS GMKGVLFRAK DAIKTKFGAR
WLPAKAKNSD FPGNWWIIET KHNVADVLAV IQQYA
