ID   PRMC_LACLA              Reviewed;         270 AA.
AC   Q9CHX0;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Release factor glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02126};
DE            Short=RF MTase {ECO:0000255|HAMAP-Rule:MF_02126};
DE            EC=2.1.1.297 {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
GN   Name=prmC {ECO:0000255|HAMAP-Rule:MF_02126}; Synonyms=hemK;
GN   OrderedLocusNames=LL0598; ORFNames=L188472;
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 [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: Methylates the class 1 translation termination release
CC       factors RF1/PrfA and RF2/PrfB on the glutamine residue of the
CC       universally conserved GGQ motif. {ECO:0000255|HAMAP-Rule:MF_02126}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC         methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC         factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC         COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61891; EC=2.1.1.297; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02126};
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. PrmC subfamily. {ECO:0000255|HAMAP-Rule:MF_02126}.
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DR   EMBL; AE005176; AAK04696.1; -; Genomic_DNA.
DR   PIR; F86699; F86699.
DR   RefSeq; NP_266754.1; NC_002662.1.
DR   RefSeq; WP_010905456.1; NC_002662.1.
DR   AlphaFoldDB; Q9CHX0; -.
DR   SMR; Q9CHX0; -.
DR   STRING; 272623.L188472; -.
DR   PaxDb; Q9CHX0; -.
DR   EnsemblBacteria; AAK04696; AAK04696; L188472.
DR   KEGG; lla:L188472; -.
DR   PATRIC; fig|272623.7.peg.638; -.
DR   eggNOG; COG2890; Bacteria.
DR   HOGENOM; CLU_018398_3_2_9; -.
DR   OMA; FDARYWE; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; HemK-like.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00536; hemK_fam; 1.
DR   TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..270
FT                   /note="Release factor glutamine methyltransferase"
FT                   /id="PRO_0000414527"
FT   BINDING         113..117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         177..180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         177
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   270 AA;  30912 MW;  3F0FF159844013F7 CRC64;
     MLWIEAVRTL SADLEDPFEL EFVWRNLHEL NKLSWLNLMR EKITDQELKL LTEVSKRLHQ
     NEPPQYIVGW AEFRDLKLKV DERVLIPRPE TEELVEMILA ENEKDSLKIL DIGTGSGAIA
     ISLAQARENW SVKASDISKE ALTLAAENAE INQANLEFIQ SDVLDKITDS FDIIVSNPPY
     IAFDETYEMD NSVIKYEPDL ALFAENQGLA IYQKIADQAV NHLTDNGKIY LEIGYKQGQA
     VQAIFQEKFT DKLVSIHQDI FGKDRMISVK