PRMA_LEPIN
ID PRMA_LEPIN Reviewed; 300 AA.
AC Q8F6B7;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=LA_1391;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN48590.1; -; Genomic_DNA.
DR RefSeq; NP_711572.1; NC_004342.2.
DR RefSeq; WP_001270455.1; NC_004342.2.
DR AlphaFoldDB; Q8F6B7; -.
DR SMR; Q8F6B7; -.
DR STRING; 189518.LA_1391; -.
DR PRIDE; Q8F6B7; -.
DR EnsemblBacteria; AAN48590; AAN48590; LA_1391.
DR GeneID; 61142230; -.
DR KEGG; lil:LA_1391; -.
DR PATRIC; fig|189518.3.peg.1386; -.
DR HOGENOM; CLU_049382_0_2_12; -.
DR InParanoid; Q8F6B7; -.
DR OMA; EFFFIFP; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..300
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_0000192276"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ SEQUENCE 300 AA; 33887 MW; 052E2332381B0D14 CRC64;
MRYREIILSI PKEIAENFTS FLDEVGVVGY YEILFDREVP RAPDEEIISD DTKFRVYLAE
EDKENETKIL IFLKATAGES FFLESRWIET KEYEEAYKEF YKPFIIGSYR VIPTWEKDTA
LGTTPEGIFP LLVNPGLAFG TGHHETTRLV LGRMGDLNLS AKRIADVGTG SGILSLAAAK
SGASLILAID VDPNSVRSAS FNRDENEISS EVLVVEEGGF DHKKIQEQTW DLLIANITFA
VLKANIQKIA SIKTDHFLFS GVITERKEEF LELLKNTVGG EGVFFREDTG WELIEWKRKG