MOM_BPMU
ID MOM_BPMU Reviewed; 241 AA.
AC P06018;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Methylcarbamoylase mom {ECO:0000303|PubMed:32369169};
DE AltName: Full=Adenine modification enzyme mom;
DE AltName: Full=Gene product 55;
DE Short=gp55;
DE AltName: Full=Gene product mom;
DE Short=gpMom;
DE AltName: Full=Modification of Mu;
DE Short=Mom;
GN Name=mom; OrderedLocusNames=Mup55;
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].
RX PubMed=6345072; DOI=10.1101/sqb.1983.047.01.075;
RA Kahmann R.;
RT "Methylation regulates the expression of a DNA-modification function
RT encoded by bacteriophage Mu.";
RL Cold Spring Harb. Symp. Quant. Biol. 47:639-646(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6229339; DOI=10.1016/0092-8674(84)90088-6;
RA Plasterk R.H.A., Vollering M., Brinkman A., van de Putte P.;
RT "Analysis of the methylation-regulated Mu mom transcript.";
RL Cell 36:189-196(1984).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=1258376; DOI=10.1016/0042-6822(76)90232-4;
RA Toussaint A.;
RT "The DNA modification function of temperate phage Mu-1.";
RL Virology 70:17-27(1976).
RN [5]
RP CHARACTERIZATION.
RX PubMed=6369315; DOI=10.1073/pnas.80.24.7400;
RA Swinton D., Hattman S., Crain P.F., Cheng C.S., Smith D.L., McCloskey J.A.;
RT "Purification and characterization of the unusual deoxynucleoside, alpha-N-
RT (9-beta-D-2'-deoxyribofuranosylpurin-6-yl)glycinamide, specified by the
RT phage Mu modification function.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:7400-7404(1983).
RN [6]
RP INDUCTION.
RX PubMed=2934296; DOI=10.1016/0378-1119(85)90108-8;
RA Kahmann R., Seiler A., Wulczyn F.G., Pfaff E.;
RT "The mom gene of bacteriophage mu: a unique regulatory scheme to control a
RT lethal function.";
RL Gene 39:61-70(1985).
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 REVIEW.
RX PubMed=7649402; DOI=10.1096/fasebj.9.11.7649402;
RA Gommers-Ampt J.H., Borst P.;
RT "Hypermodified bases in DNA.";
RL FASEB J. 9:1034-1042(1995).
RN [9]
RP INDUCTION.
RX PubMed=9336472; DOI=10.1093/nar/25.21.4385;
RA Hattman S., Sun W.;
RT "Escherichia coli OxyR modulation of bacteriophage Mu mom expression in
RT dam+ cells can be attributed to its ability to bind hemimethylated Pmom
RT promoter DNA.";
RL Nucleic Acids Res. 25:4385-4388(1997).
RN [10]
RP REVIEW.
RX PubMed=10665835; DOI=10.1016/s0163-7258(99)00042-x;
RA Hattman S.;
RT "Unusual transcriptional and translational regulation of the bacteriophage
RT Mu mom operon.";
RL Pharmacol. Ther. 84:367-388(1999).
RN [11]
RP FUNCTION.
RX PubMed=18204304; DOI=10.4161/cc.7.1.5158;
RA Kaminska K.H., Bujnicki J.M.;
RT "Bacteriophage Mu Mom protein responsible for DNA modification is a new
RT member of the acyltransferase superfamily.";
RL Cell Cycle 7:120-121(2008).
RN [12]
RP INDUCTION.
RX PubMed=22287621; DOI=10.1093/nar/gks037;
RA Karambelkar S., Swapna G., Nagaraja V.;
RT "Silencing of toxic gene expression by Fis.";
RL Nucleic Acids Res. 40:4358-4367(2012).
RN [13]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-58; TYR-59;
RP ARG-111; SER-124; ASP-149 AND TYR-159.
RX PubMed=32369169; DOI=10.1093/nar/gkaa319;
RA Karambelkar S., Udupa S., Gowthami V.N., Ramachandra S.G., Swapna G.,
RA Nagaraja V.;
RT "Emergence of a novel immune-evasion strategy from an ancestral protein
RT fold in bacteriophage Mu.";
RL Nucleic Acids Res. 48:5294-5305(2020).
CC -!- FUNCTION: Iron-binding protein that performs methylcarbamoylation of
CC adenine using acetyl CoA (PubMed:32369169). This chemical modificaltion
CC makes the viral DNA resistant to a variety of host type I and type II
CC restriction enzymes by modifying approximately 15% of DNA adenine
CC residues (PubMed:32369169). The modification called momylation changes
CC adenine for N6-methylcarbamoyl adenine and occurs just before packaging
CC (PubMed:1258376, PubMed:32369169). Target sequences are 5'-(C or G)-A-
CC (Cor G)-N-(C or T)-3' (PubMed:1258376). Also usually modifies adenine
CC residues in the host cellular DNA (PubMed:1258376).
CC {ECO:0000269|PubMed:1258376, ECO:0000269|PubMed:32369169}.
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:0000269|PubMed:32369169};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Note=Mn(2+), Zn(2+), Mg(2+), Ca(2+), Co(2+) and Cu(2+) showed
CC undetectable interaction. {ECO:0000269|PubMed:32369169};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
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. {ECO:0000269|PubMed:22287621,
CC ECO:0000269|PubMed:2934296, ECO:0000269|PubMed:8293968,
CC ECO:0000269|PubMed:9336472}.
CC -!- SIMILARITY: Belongs to the mulikevirus mom protein family.
CC {ECO:0000305}.
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DR EMBL; V01463; CAA24710.1; -; Genomic_DNA.
DR EMBL; AF083977; AAF01131.1; -; Genomic_DNA.
DR PIR; B21135; ZQBPMU.
DR RefSeq; NP_050657.1; NC_000929.1.
DR GeneID; 2636302; -.
DR KEGG; vg:2636302; -.
DR Proteomes; UP000002611; 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 1: Evidence at protein 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..241
FT /note="Methylcarbamoylase mom"
FT /id="PRO_0000077664"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:32369169"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:32369169"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:32369169"
FT MUTAGEN 58
FT /note="H->A: Loss of acetyl CoA-binding."
FT /evidence="ECO:0000269|PubMed:32369169"
FT MUTAGEN 59
FT /note="Y->A: Loss of iron- and acetyl CoA-binding."
FT /evidence="ECO:0000269|PubMed:32369169"
FT MUTAGEN 111
FT /note="R->A: No effect on iron-binding or acetyl CoA-
FT binding."
FT /evidence="ECO:0000269|PubMed:32369169"
FT MUTAGEN 124
FT /note="S->A: Loss of acetyl CoA-binding."
FT /evidence="ECO:0000269|PubMed:32369169"
FT MUTAGEN 149
FT /note="D->A: Loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:32369169"
FT MUTAGEN 159
FT /note="Y->A: Loss of iron- and acetyl CoA-binding."
FT /evidence="ECO:0000269|PubMed:32369169"
SQ SEQUENCE 241 AA; 28278 MW; 73621DE0976975E4 CRC64;
MPASIPRRNI VGKEKKSRIL TKPCVIEYEG QIVGYGSKEL RVETISCWLA RTIIQTKHYS
RRFVNNSYLH LGVFSGRDLV GVLQWGYALN PNSGRRVVLE TDNRGYMELN RMWLHDDMPR
NSESRAISYA LKVIRLLYPS VEWVQSFADE RCGRAGVVYQ ASNFDFIGSH ESTFYELDGE
WYHEITMNAI KRGGQRGVYL RANKERAVVH KFNQYRYIRF LNKRARKRLN TKLFKVQPYP
K
