PRMA_METFK
ID PRMA_METFK Reviewed; 295 AA.
AC Q1GX86;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Mfla_0023;
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-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; CP000284; ABE48294.1; -; Genomic_DNA.
DR RefSeq; WP_011478391.1; NC_007947.1.
DR AlphaFoldDB; Q1GX86; -.
DR SMR; Q1GX86; -.
DR STRING; 265072.Mfla_0023; -.
DR EnsemblBacteria; ABE48294; ABE48294; Mfla_0023.
DR KEGG; mfa:Mfla_0023; -.
DR eggNOG; COG2264; Bacteria.
DR HOGENOM; CLU_049382_4_1_4; -.
DR OMA; EFFFIFP; -.
DR OrthoDB; 1712450at2; -.
DR Proteomes; UP000002440; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..295
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_1000046047"
FT BINDING 150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ SEQUENCE 295 AA; 31698 MW; 317847F52EFC19A7 CRC64;
MAWISLRIDA RDDNAELLSD TLMELGALSA SIEDANAETP DEQPIFGEPG DPPPGIWQQN
VVTALLDESA DLDSLLEELS AATGITDFRY STETIAEQDW VRATQSQFEP IRIRDDLWIV
PSWHDAPNPD GLNIVLDPGL AFGTGSHPTT HLCLSWLADT VKPDTSVLDY GCGSGILAIA
ARKLGAGKVV GVDIDAQAIQ SSVYNADQNQ VDASFYLASD LPGGQFDIVV ANILSSALSV
LAPALARAAR SGGRIALSGI LREQADQVSA IYQEWFEMDA PVFMDSWVLL TGSRR
