ID   MENG_LACLA              Reviewed;         252 AA.
AC   P49016;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Demethylmenaquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01813};
DE            EC=2.1.1.163 {ECO:0000255|HAMAP-Rule:MF_01813};
GN   Name=menG {ECO:0000255|HAMAP-Rule:MF_01813}; Synonyms=menH;
GN   OrderedLocusNames=LL1669.1;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C2;
RX   PubMed=8366036; DOI=10.1128/jb.175.17.5510-5519.1993;
RA   Geller B.L., Ivey R.G., Trempy J.E., Hettinger-Smith B.;
RT   "Cloning of a chromosomal gene required for phage infection of Lactococcus
RT   lactis subsp. lactis C2.";
RL   J. Bacteriol. 175:5510-5519(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Methyltransferase required for the conversion of
CC       demethylmenaquinol (DMKH2) to menaquinol (MKH2). {ECO:0000255|HAMAP-
CC       Rule:MF_01813}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-demethylmenaquinol + S-adenosyl-L-methionine = a
CC         menaquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42640,
CC         Rhea:RHEA-COMP:9539, Rhea:RHEA-COMP:9563, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18151, ChEBI:CHEBI:55437, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789; EC=2.1.1.163; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01813};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis;
CC       menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01813}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_01813}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE005176; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L14679; AAA03166.1; -; Unassigned_DNA.
DR   EMBL; AE005176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B48653; B48653.
DR   AlphaFoldDB; P49016; -.
DR   SMR; P49016; -.
DR   UniPathway; UPA00079; UER00169.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0043770; F:demethylmenaquinone methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102094; F:S-adenosylmethionine:2-demethylmenaquinol methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102955; F:S-adenosylmethionine:2-demethylmenaquinol-7 methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102027; F:S-adenosylmethionine:2-demethylquinol-8 methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR   InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR   Pfam; PF01209; Ubie_methyltran; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1.
DR   PROSITE; PS51608; SAM_MT_UBIE; 1.
DR   PROSITE; PS01183; UBIE_1; 1.
DR   PROSITE; PS01184; UBIE_2; 1.
PE   3: Inferred from homology;
KW   Menaquinone biosynthesis; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..252
FT                   /note="Demethylmenaquinone methyltransferase"
FT                   /id="PRO_0000193284"
FT   BINDING         64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT   BINDING         112..113
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT   CONFLICT        5
FT                   /note="K -> M (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120..122
FT                   /note="KGS -> NEN (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="L -> F (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="Q -> K (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   252 AA;  28449 MW;  7D971E3A4BD804ED CRC64;
     MCYNKSMTKV NEERVQEIFN SISSDYDKMN AIISFKQHDL WRAKTMKRMG DLTGLSILDL
     CCGTGDWTFD LSESVGPSGK VIGLDFSENM LEIAKAKLKE EAKKNIEFLQ GNAMALPFEK
     GSFDVVTIGY GLRNTPDYLT VLKEIFRVLK PGGRVVCIET SHPTLPIYKQ AFELYFKNVM
     PFLGKVFAKS LKEYQWLQKS AEDFPDAKTL EELFRKAGFV AVEYQKHGGG AIASHFATKS
     QKPKSNIRIG KK