ID PRMA_LEPBJ Reviewed; 300 AA. AC Q04QV8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 02-JUN-2021, 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}; OrderedLocusNames=LBJ_2231; OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197). OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=355277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JB197; RX PubMed=16973745; DOI=10.1073/pnas.0603979103; RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., RA Rood J.I., Davies J.K., Adler B.; RT "Genome reduction in Leptospira borgpetersenii reflects limited RT transmission potential."; RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000350; ABJ76712.1; -; Genomic_DNA. DR RefSeq; WP_002725156.1; NC_008510.1. DR EnsemblBacteria; ABJ76712; ABJ76712; LBJ_2231. DR GeneID; 61174921; -. DR KEGG; lbj:LBJ_2231; -. DR HOGENOM; CLU_049382_0_2_12; -. DR OMA; EFFFIFP; -. DR BioCyc; LBOR355277:G1G6G-2559-MONOMER; -. DR Proteomes; UP000000656; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-UniRule. DR HAMAP; MF_00735; Methyltr_PrmA; 1. DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase. DR InterPro; IPR029063; SAM-dependent_MTases. 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..300 FT /note="Ribosomal protein L11 methyltransferase" FT /id="PRO_1000046042" FT BINDING 147 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735" FT BINDING 168 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735" FT BINDING 190 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735" FT BINDING 236 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735" SQ SEQUENCE 300 AA; 33743 MW; 959165C6336F016B CRC64; MKYREIILNI PKEIAEDFTT FLDEIGVAGY YEILFDREVP RAPHEEIISD DTKFRVYLAQ EDNENETKIL IYLKANAGEV FFSESRWIET KEYEEAYKEF YKPFIVGSYR VIPTWEKDTA LGTTPEGIFP LFINPGLAFG TGHHETTRLV LGRMGNLSLS GKKVVDVGTG SGILSVAAAK SGASPILAVD VDPNSVRSAS FNRDENDISS EVLAVEEGGF DHEKIQGQTW DLLIANITFA VLKANIQKIV SIKTDHFLFS GVITERLEEF LELLKNEVGG EGVFFQEDTG WELIEWKRKG //