MOM_BPD10
ID MOM_BPD10 Reviewed; 245 AA.
AC P08794; C9DGR4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Methylcarbamoylase mom {ECO:0000250|UniProtKB:P06018};
DE AltName: Full=Adenine modification enzyme mom;
DE AltName: Full=Gene product mom;
DE Short=gpMom;
DE AltName: Full=Modification of Mu;
DE Short=Mom;
GN Name=mom;
OS Escherichia phage D108 (Bacteriophage D108).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus; unclassified Muvirus.
OX NCBI_TaxID=665033;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kropinski A.M., Villegas A., Lingohr E.J.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 177-238.
RX PubMed=2957646; DOI=10.1093/nar/15.16.6691;
RA Szatmari G.B., Lapointe M., Dubow M.S.;
RT "The right end of transposable bacteriophage D108 contains a 520 base pair
RT protein-encoding sequence not present in bacteriophage Mu.";
RL Nucleic Acids Res. 15:6691-6704(1987).
CC -!- FUNCTION: Iron-binding protein that performs methylcarbamoylation of
CC adenine using acetyl CoA. This chemical modificaltion makes the viral
CC DNA resistant to a variety of host type I and type II restriction
CC enzymes by modifying approximately 15% of DNA adenine residues. The
CC modification called momylation changes adenine for N6-methylcarbamoyl
CC adenine and occurs just before packaging. Target sequences are 5'-(C or
CC G)-A-(Cor G)-N-(C or T)-3'. Also usually modifies adenine residues in
CC the host cellular DNA. {ECO:0000250|UniProtKB:P06018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + acetyl-CoA + AH2 + NH4(+) + O2 =
CC A + a N(6)-methylcarbamoyl-2'-deoxyadenosine in DNA + CoA + H(+) + 2
CC H2O; Xref=Rhea:RHEA:65948, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:16940, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:90615,
CC ChEBI:CHEBI:166827; Evidence={ECO:0000250|UniProtKB:P06018};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P06018};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:P06018};
CC Note=Mn(2+), Zn(2+), Mg(2+), Ca(2+), Co(2+) and Cu(2+) showed
CC undetectable interaction. {ECO:0000250|UniProtKB:P06018};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC Mom gene must be expressed very efficiently only at a very late stage
CC in the lytic cycle because its expression is lethal to the host cell.
CC Expression of Mom requires the viral late transcription activator C and
CC the host deoxyadenosine methylase Dam. Dam methylates three viral sites
CC upstream of the mom promoter to prevent binding of the host
CC translational repressor OxyR. If the viral sites are not fully
CC methylated, the host translational repressor OxyR prevents RNAP
CC recruitment by the transactivator C. Host Fis protein might also act as
CC a negative regulator of mom gene expression. Mom expression is further
CC controlled on the translation level by the viral translational
CC activator Com.
CC -!- SIMILARITY: Belongs to the mulikevirus mom protein family.
CC {ECO:0000305}.
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DR EMBL; GQ357916; ACV50315.1; -; Genomic_DNA.
DR EMBL; X05927; CAA29368.1; -; Genomic_DNA.
DR PIR; S07973; S07973.
DR RefSeq; YP_003335804.1; NC_013594.1.
DR GeneID; 8658867; -.
DR KEGG; vg:8658867; -.
DR Proteomes; UP000000320; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Host cytoplasm; Host-virus interaction; Iron; Late protein; Metal-binding;
KW Reference proteome; Restriction-modification system evasion by virus;
KW Transferase.
FT CHAIN 1..245
FT /note="Methylcarbamoylase mom"
FT /id="PRO_0000077663"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06018"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06018"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P06018"
FT CONFLICT 194
FT /note="G -> E (in Ref. 2; CAA29368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 28730 MW; 7C654411D5B973C4 CRC64;
MPASIPRRNI VGKEKKSRIL TKPCVIEYEG QIVGYGSKEL RVETISCWLA RTIIQTKHYS
RRFVNNSYLH LGVFSGRDLV GVLQWGYALN PNSGRRVVLE TDNRGYMELN RMWLHDDMPR
NSESRAISYA LKTIRLLYPS VEWVQSFADE RCGRAGVVYQ ASNFDFIGSH ESTFYELDGE
WYHEITMNAI KRGGQRGMYL RANKERAVVH KFNQYRYIRF LNKRARKRLN TKLFRIQPYP
KSSSD
