ID   PRMA_CAMJJ              Reviewed;         281 AA.
AC   A1W0A4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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};
GN   OrderedLocusNames=CJJ81176_1135;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) 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; CP000538; EAQ72083.1; -; Genomic_DNA.
DR   RefSeq; WP_002853953.1; NC_008787.1.
DR   AlphaFoldDB; A1W0A4; -.
DR   SMR; A1W0A4; -.
DR   STRING; 354242.CJJ81176_1135; -.
DR   EnsemblBacteria; EAQ72083; EAQ72083; CJJ81176_1135.
DR   KEGG; cjj:CJJ81176_1135; -.
DR   eggNOG; COG2264; Bacteria.
DR   HOGENOM; CLU_049382_1_0_7; -.
DR   OMA; EFFFIFP; -.
DR   Proteomes; UP000000646; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..281
FT                   /note="Ribosomal protein L11 methyltransferase"
FT                   /id="PRO_1000046004"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         175
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         216
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   281 AA;  32329 MW;  F85544B5D5A427D6 CRC64;
     MQKKYYELFF IVEERYKNLF LDFAFDLGIE AIEEKDNGVY IRSHESLEDL SWALEIFAQK
     LTTTFNLNHK IISNLSLVEK ENKDWIQEYK KGIKPILVDN VYIHTTWQEE KKNCINIKIN
     PALAFGSGHH ESTYSCVKFL QKFSKSKLRA LDLGCGSGIL GIIMAKFGCN VEICDTDELA
     IDSSLENARL NGVDFYKAWC GSIDKANGLY NLIVANIIAD VILILEKDIK NHLEDNAILI
     LSGILDKYST RIKEKFQDLE LIDEMQINEW CSFVYKNNKK G