ID   PRMA_STAAU              Reviewed;         312 AA.
AC   P0A0P5; P45557;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=912;
RX   PubMed=8045913; DOI=10.1128/jb.176.15.4779-4783.1994;
RA   Ohta T., Saito K., Kuroda M., Honda K., Hirata H., Hayashi H.;
RT   "Molecular cloning of two new heat shock genes related to the hsp70 genes
RT   in Staphylococcus aureus.";
RL   J. Bacteriol. 176:4779-4783(1994).
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   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC       {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305}.
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DR   EMBL; D30690; BAA06361.1; -; Genomic_DNA.
DR   RefSeq; WP_001104607.1; NZ_WYDB01000002.1.
DR   AlphaFoldDB; P0A0P5; -.
DR   SMR; P0A0P5; -.
DR   OMA; EFFFIFP; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Stress response;
KW   Transferase.
FT   CHAIN           1..312
FT                   /note="Ribosomal protein L11 methyltransferase"
FT                   /id="PRO_0000192307"
FT   BINDING         160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         203
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT   BINDING         246
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   312 AA;  35527 MW;  C53CA8BF1489A980 CRC64;
     MNWTELSIII NHEAVELATN ILENHGSNGV VIEDSDDLIN QPEDKYGEIY ALKKEDYPDK
     GVRLKAYFNE MTYDDKLRQQ IKDELLNLDE LDQHNIQFSE QIIAETDWEN EWKNYFHPFR
     ASKKFTIVPS WETYAKEADE ELCIELDPGM AFGTGDHPTT SMCLKAIETY VLPQHSVIDV
     GTGSGILSIA SHLIGVKRIK ALDIDEMAVS VAKENFRRNH CETLIEAVPG NLLKDETEKF
     DIVIANILAH IIDEMIEDAY NTLNEGGYFI TSGIIKEKYE GIQSHMERVG FKIISEQHDN
     GWVCLVGQKV SE