ID A3CKJ5_STRSV Unreviewed; 318 AA.
AC A3CKJ5;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735};
DE Short=L11 Mtase {ECO:0000256|HAMAP-Rule:MF_00735};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00735};
GN Name=prmA {ECO:0000256|HAMAP-Rule:MF_00735,
GN ECO:0000313|EMBL:ABN43700.1};
GN OrderedLocusNames=SSA_0241 {ECO:0000313|EMBL:ABN43700.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN43700.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN43700.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN43700.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00735};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000256|ARBA:ARBA00009741, ECO:0000256|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; CP000387; ABN43700.1; -; Genomic_DNA.
DR RefSeq; WP_002903455.1; NC_009009.1.
DR RefSeq; YP_001034250.1; NC_009009.1.
DR AlphaFoldDB; A3CKJ5; -.
DR STRING; 388919.SSA_0241; -.
DR KEGG; ssa:SSA_0241; -.
DR PATRIC; fig|388919.9.peg.234; -.
DR eggNOG; COG2264; Bacteria.
DR HOGENOM; CLU_049382_0_1_9; -.
DR OrthoDB; 9785995at2; -.
DR Proteomes; UP000002148; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:RHEA.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00735; Methyltr_PrmA; 1.
DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00406; prmA; 1.
DR PANTHER; PTHR43648; ELECTRON TRANSFER FLAVOPROTEIN BETA SUBUNIT LYSINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43648:SF1; ELECTRON TRANSFER FLAVOPROTEIN BETA SUBUNIT LYSINE METHYLTRANSFERASE; 1.
DR Pfam; PF06325; PrmA; 1.
DR PIRSF; PIRSF000401; RPL11_MTase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735,
KW ECO:0000313|EMBL:ABN43700.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002148};
KW Ribonucleoprotein {ECO:0000313|EMBL:ABN43700.1};
KW Ribosomal protein {ECO:0000313|EMBL:ABN43700.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:ABN43700.1}.
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ SEQUENCE 318 AA; 34978 MW; 964EAFE988172936 CRC64;
MMDTWQELTI EVKREAEEAA SNILIELGSQ GVAIDDSADY LGQVDQYGEL FPEVEQSERV
KVTGYYPDSV DIEAIAAQAN ERLAELDGFG LETGDIQLTR QELAEEDWAD NWKKYFEPAR
ITHDLTIVPS WTEYEATAGE KIIKLDPGMA FGTGTHPTTK MSLFALEQVL RGGETVLDVG
TGSGVLSIAS SLLGAKDIYA YDLDEVAVRV VQENIELNPG MENIHVAPGD LLRGVEIKAD
VIVANILADI LVHLTEDAYR LVKDEGYLIM SGIISEKWEM VRESAEAAGF FLETHMIQGE
WNACVFKKTQ DISGVIGG
//
