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Database: UniProt
Entry: A0A0G9F8M9_LACPN
LinkDB: A0A0G9F8M9_LACPN
Original site: A0A0G9F8M9_LACPN 
ID   A0A0G9F8M9_LACPN        Unreviewed;       288 AA.
AC   A0A0G9F8M9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Release factor glutamine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126};
DE            Short=RF MTase {ECO:0000256|HAMAP-Rule:MF_02126};
DE            EC=2.1.1.297 {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
GN   Name=hemK {ECO:0000313|EMBL:ODO62194.1};
GN   Synonyms=prmC {ECO:0000256|HAMAP-Rule:MF_02126,
GN   ECO:0000313|EMBL:QHM48156.1};
GN   ORFNames=ASV54_09745 {ECO:0000313|EMBL:APD01610.1}, AVR83_10875
GN   {ECO:0000313|EMBL:AOB23423.1}, C7M40_00054
GN   {ECO:0000313|EMBL:QHM48156.1}, LPJSA22_02199
GN   {ECO:0000313|EMBL:ODO62194.1};
OS   Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1590 {ECO:0000313|EMBL:ODO62194.1, ECO:0000313|Proteomes:UP000094892};
RN   [1] {ECO:0000313|Proteomes:UP000183026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF1298 {ECO:0000313|Proteomes:UP000183026};
RA   McLeod A., Rud I., Axelsson L.;
RT   "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT   associated with unfavorable effect.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOB23423.1, ECO:0000313|Proteomes:UP000093296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF {ECO:0000313|EMBL:AOB23423.1,
RC   ECO:0000313|Proteomes:UP000093296};
RA   Petkau K., Fast D., Duggal A., Foley E.;
RT   "Comparative evaluation of the genomes of common bacterial members of the
RT   Drosophila intestinal community.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ODO62194.1, ECO:0000313|Proteomes:UP000094892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSA22 {ECO:0000313|EMBL:ODO62194.1,
RC   ECO:0000313|Proteomes:UP000094892};
RA   Choi H.S.;
RT   "Genome sequencing of Lactobacillus plantarum JSA22, isolated from
RT   fermented soybean paste.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:QHM48156.1, ECO:0000313|Proteomes:UP000465032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRCM101518 {ECO:0000313|EMBL:QHM48156.1,
RC   ECO:0000313|Proteomes:UP000465032};
RA   Jeong D.-Y.;
RT   "Lactobacillus plantatrum SRCM101518 having antimicrbial activity species
RT   isolated from Korea kimchi.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:APD01610.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MF1298 {ECO:0000313|EMBL:APD01610.1};
RA   McLeod A., Fagerlund A., Rud I., Axelsson L.;
RT   "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT   associated with unfavorable effect.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000932, ECO:0000256|HAMAP-
CC         Rule:MF_02126};
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. PrmC subfamily. {ECO:0000256|HAMAP-Rule:MF_02126}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02126}.
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DR   EMBL; CP013753; AOB23423.1; -; Genomic_DNA.
DR   EMBL; CP013149; APD01610.1; -; Genomic_DNA.
DR   EMBL; MCOL01000001; ODO62194.1; -; Genomic_DNA.
DR   EMBL; CP028241; QHM48156.1; -; Genomic_DNA.
DR   RefSeq; WP_003641434.1; NZ_WWDD01000002.1.
DR   GeneID; 77215752; -.
DR   PATRIC; fig|1590.142.peg.2189; -.
DR   OMA; FDARYWE; -.
DR   Proteomes; UP000093296; Chromosome.
DR   Proteomes; UP000094892; Unassembled WGS sequence.
DR   Proteomes; UP000183026; Chromosome.
DR   Proteomes; UP000465032; 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00536; hemK_fam; 1.
DR   NCBIfam; TIGR03534; RF_mod_PrmC; 1.
DR   PANTHER; PTHR18895; HEMK METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR18895:SF74; MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_02126};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_02126};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02126}.
FT   DOMAIN          11..79
FT                   /note="Release factor glutamine methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17827"
FT   DOMAIN          111..201
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   BINDING         124..128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         189..192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         189
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   288 AA;  31637 MW;  AFFA16EBCCB7D662 CRC64;
     MNKPTQPTYF EAQQWASFCL KTAQLPTDSA RFLLLGLSRL DQTQLLIRYR EPLPSAVWHA
     YQQGIDRVVA GEPVQYVLGD APFYGLTLQV DPAVLIPRVE TEELVDWILT DVPATAPVRL
     LDVGTGSGAI ALAIKHERPA WEITASDIST AALQVAKANA DRLHLDVKLV HSDLLTSVSA
     QPFDIIVSNP PYIAASEKDV MDASVLAHEP QTALFADHDG LALYEQLATT VADHLTSTGR
     LYLEFGYHQG PALQTLFAQS MPDATVTLRQ DMAGHNRMLR VAMTLTRQ
//
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