ID   PRMA_LISM4              Reviewed;         314 AA.
AC   G2K044; Q9S5A2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00735};
DE            Short=L11 Mtase {ECO:0000255|HAMAP-Rule:MF_00735};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00735};
GN   Name=prmA {ECO:0000255|HAMAP-Rule:MF_00735}; OrderedLocusNames=LMRG_00924;
OS   Listeria monocytogenes serotype 1/2a (strain 10403S).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=393133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=10403S;
RX   PubMed=10701836; DOI=10.1379/1466-1268(2000)005<0021:csatao>2.0.co;2;
RA   Hanawa T., Kai M., Kamiya S., Yamamoto T.;
RT   "Cloning, sequencing, and transcriptional analysis of the dnaK heat shock
RT   operon of Listeria monocytogenes.";
RL   Cell Stress Chaperones 5:21-29(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10403S;
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M.,
RA   Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D.,
RA   Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B., Chen Z.,
RA   Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L.,
RA   Lui A., MacDonald J., Mehta T., Montmayeur A., Neiman D., Park D.,
RA   Pearson M., Priest M., Richards J., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Listeria monocytogenes strain 10403S.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000255|HAMAP-
CC       Rule:MF_00735}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00735};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00735}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC       {ECO:0000255|HAMAP-Rule:MF_00735}.
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DR   EMBL; AB023064; BAA82791.1; -; Genomic_DNA.
DR   EMBL; CP002002; AEO06456.1; -; Genomic_DNA.
DR   PIR; T43740; T43740.
DR   RefSeq; WP_010990133.1; NC_017544.1.
DR   AlphaFoldDB; G2K044; -.
DR   SMR; G2K044; -.
DR   EnsemblBacteria; AEO06456; AEO06456; LMRG_00924.
DR   KEGG; lmt:LMRG_00924; -.
DR   HOGENOM; CLU_049382_0_1_9; -.
DR   OMA; EFFFIFP; -.
DR   Proteomes; UP000001288; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00735; Methyltr_PrmA; 1.
DR   InterPro; IPR004498; Ribosomal_PrmA_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PIRSF; PIRSF000401; RPL11_MTase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00406; prmA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..314
FT                   /note="Ribosomal protein L11 methyltransferase"
FT                   /id="PRO_0000419032"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         182
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         204
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   314 AA;  34811 MW;  E71F4AF1DDF437F6 CRC64;
     MEWSEVEVHT TNEAVEPVAN VLTEFGAAGV SIEDVADFLR EREDKFGEIY ALRREDYPED
     GVIIKAYFLK TTEFVEQIPE IEQTLKNLST FDIPLGKFQF VVNDVDDEEW ATAWKKYYHP
     VQITDRITIV PSWESYTPSA NEIIIELDPG MAFGTGTHPT TQLCIRALSN YLQPGDEVID
     VGTGSGVLSI ASAKLGAKSI LATDLDEIAT RAAEENITLN KTEHIITVKQ NNLLQDINKT
     NVDIVVANIL AEVILLFPED VYKALKPGGV FIASGIIEDK AKVVEEALKN AGLIIEKMEQ
     QGDWVAIISK RGVE