CIRCN_BPMU
ID CIRCN_BPMU Reviewed; 495 AA.
AC P08557; Q9T1V5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA circularization protein N;
DE AltName: Full=64 kDa virion protein;
DE AltName: Full=Gene product 43;
DE Short=gp43;
DE AltName: Full=Gene product N;
DE Short=gpN;
GN Name=N; OrderedLocusNames=Mup43;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MUCTS62PAP1;
RX PubMed=2968539; DOI=10.1093/nar/16.11.5211;
RA Chaconas G., Gloor G.;
RT "Sequence of bacteriophage Mu N and P genes.";
RL Nucleic Acids Res. 16:5211-5212(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=3904174; DOI=10.1016/0042-6822(85)90388-5;
RA Grundy F.J., Howe M.M.;
RT "Morphogenetic structures present in lysates of amber mutants of
RT bacteriophage Mu.";
RL Virology 143:485-504(1985).
RN [4]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=6306260; DOI=10.1016/s0022-2836(83)80343-x;
RA Harshey R.M., Bukhari A.I.;
RT "Infecting bacteriophage mu DNA forms a circular DNA-protein complex.";
RL J. Mol. Biol. 167:427-441(1983).
RN [5]
RP FUNCTION.
RX PubMed=11894948; DOI=10.1002/j.1460-2075.1983.tb01429.x;
RA Puspurs A.H., Trun N.J., Reeve J.N.;
RT "Bacteriophage Mu DNA circularizes following infection of Escherichia
RT coli.";
RL EMBO J. 2:345-352(1983).
RN [6]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=3023361; DOI=10.1016/s0021-9258(18)66619-0;
RA Gloor G., Chaconas G.;
RT "The bacteriophage Mu N gene encodes the 64-kDa virion protein which is
RT injected with, and circularizes, infecting Mu DNA.";
RL J. Biol. Chem. 261:16682-16688(1986).
RN [7]
RP INDUCTION.
RX PubMed=8293968; DOI=10.1093/genetics/135.3.619;
RA Chiang L.W., Howe M.M.;
RT "Mutational analysis of a C-dependent late promoter of bacteriophage Mu.";
RL Genetics 135:619-629(1993).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8599204; DOI=10.1006/viro.1996.0107;
RA Grimaud R.;
RT "Bacteriophage Mu head assembly.";
RL Virology 217:200-210(1996).
RN [9]
RP REGION LYSM-LIKE.
RX PubMed=24097944; DOI=10.1128/jb.00805-13;
RA Maxwell K.L., Fatehi Hassanabad M., Chang T., Pirani N., Bona D.,
RA Edwards A.M., Davidson A.R.;
RT "Structural and functional studies of gpX of Escherichia coli phage P2
RT reveal a widespread role for LysM domains in the baseplates of contractile-
RT tailed phages.";
RL J. Bacteriol. 195:5461-5468(2013).
RN [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=27555589; DOI=10.1073/pnas.1607966113;
RA Buettner C.R., Wu Y., Maxwell K.L., Davidson A.R.;
RT "Baseplate assembly of phage Mu: Defining the conserved core components of
RT contractile-tailed phages and related bacterial systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10174-10179(2016).
CC -!- FUNCTION: Required for tail assembly of phage Mu and responsible for
CC circularizing the viral DNA after it has been ejected into the host
CC cell. Following infection, the circularized DNA can be isolated as a
CC supercoiled, non-covalent protein-DNA complex, in which the protein N
CC is bound to the ends of the DNA. Protects linear double-stranded DNA of
CC viral genome from host exonuclease degradation.
CC {ECO:0000269|PubMed:11894948, ECO:0000269|PubMed:3023361,
CC ECO:0000269|PubMed:6306260}.
CC -!- SUBUNIT: Part of a complex composed of three DNA circularization
CC protein N, three baseplate hub protein gp44 and three sub-complex wedge
CC (made of two copies of each baseplate protein gp46, gp47 and gp48) that
CC forms the baseplate. {ECO:0000269|PubMed:27555589}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27555589,
CC ECO:0000269|PubMed:8599204}. Host cytoplasm
CC {ECO:0000305|PubMed:8599204}. Note=Baseplate protein.
CC {ECO:0000269|PubMed:27555589}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC Expression of late genes is activated by the viral late transcription
CC activator C. {ECO:0000269|PubMed:8293968}.
CC -!- DOMAIN: LysM-like fold region might interact with peptidoglycan to
CC facilitate DNA ejection.
CC -!- DISRUPTION PHENOTYPE: No tail is synthesized.
CC {ECO:0000269|PubMed:3904174}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA29955.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X06796; CAA29955.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF083977; AAF01121.1; -; Genomic_DNA.
DR PIR; S01890; ZNBPMU.
DR RefSeq; NP_050647.1; NC_000929.1.
DR GeneID; 2636283; -.
DR KEGG; vg:2636283; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0099016; P:evasion by virus of DNA end degradation; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0099009; P:viral genome circularization; IEA:UniProtKB-KW.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR InterPro; IPR009826; DNA_circ_N.
DR Pfam; PF07157; DNA_circ_N; 1.
PE 1: Evidence at protein level;
KW DNA end degradation evasion by virus; DNA-binding; Host cytoplasm;
KW Host-virus interaction; Late protein; Reference proteome;
KW Viral genome circularization; Viral release from host cell;
KW Viral tail assembly; Virion; Virus entry into host cell.
FT CHAIN 1..495
FT /note="DNA circularization protein N"
FT /id="PRO_0000077690"
FT DNA_BIND 407..426
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 331..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..493
FT /note="LysM-like"
FT COMPBIAS 335..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 35
FT /note="V -> VI (in Ref. 1; CAA29955)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="G -> GP (in Ref. 1; CAA29955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 52041 MW; DF9D4FA3B157007B CRC64;
MFEDALNAVN AVRDKTGGGR KTTGKGTFRN VPFLVIEEQK QAGGRRLVKR EYPLRDTGGV
NDLGKKLRSR TFSACILNSN AETARDEAGA LMDALDAPGS GELVHPDFGT VDVMVDSWEC
RTKADELNYY AFTVTVYPSL QDTAPDAETD TSAAVPAQAV AVTGSLGDTL SSVWQTVKDG
TAAATAVMEA VTGVIDDISD AVDNLGVTQT VSGLMGSLSA MKGSVTSLIN QPAMLASSLM
GALSGVSSLC DTRTAFSTWN RLAQRFERRH AATAGRQGTI TTSYNSPVAE KNIATLNYVM
LAAAQTYRAE AASQALTAAL DFSRRMDNAA RAPVLDAPST TTGTASGASS TSATVTQGQL
QLTAITPDGG FSQVSFSDSG TATPPVFESV SDIEKTTAML GAALDSVILT ASEQGFSTDS
VQLTQLRLLV VADLEKRGLQ LAGSESHHLP ETLPAMVALY RFTGNSRNWQ RLARRNGISN
PLFVPGGVSI EVINE
