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Database: UniProt
Entry: M5J5Q6_9LACO
LinkDB: M5J5Q6_9LACO
Original site: M5J5Q6_9LACO 
ID   M5J5Q6_9LACO            Unreviewed;       293 AA.
AC   M5J5Q6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:EKW98465.1};
GN   ORFNames=D271_05635 {ECO:0000313|EMBL:EKW98465.1};
OS   Ligilactobacillus saerimneri 30a.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW98465.1, ECO:0000313|Proteomes:UP000011912};
RN   [1] {ECO:0000313|EMBL:EKW98465.1, ECO:0000313|Proteomes:UP000011912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30a {ECO:0000313|EMBL:EKW98465.1,
RC   ECO:0000313|Proteomes:UP000011912};
RX   PubMed=23405290;
RA   Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA   Lolkema J.S., Lucas P.M.;
RT   "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT   sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT   Biogenic Amines.";
RL   Genome Announc. 1:E00097-E00012(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKW98465.1}.
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DR   EMBL; ANAG01000017; EKW98465.1; -; Genomic_DNA.
DR   RefSeq; WP_009554288.1; NZ_ANAG01000017.1.
DR   AlphaFoldDB; M5J5Q6; -.
DR   STRING; 1227363.D271_05635; -.
DR   GeneID; 80987005; -.
DR   PATRIC; fig|1227363.6.peg.1101; -.
DR   Proteomes; UP000011912; Unassembled WGS sequence.
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:EKW98465.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011912};
KW   Ribonucleoprotein {ECO:0000313|EMBL:EKW98465.1};
KW   Ribosomal protein {ECO:0000313|EMBL:EKW98465.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:EKW98465.1}.
FT   BINDING         140
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   293 AA;  32158 MW;  1356F28F186EA116 CRC64;
     MDWNELVIVT SNEAIEAVSN ILMEEGAGGV QIDDQDPQAV RVITYFTADS PLNELLPKLK
     EKVHGLKKYG INPEPGQVFL TNIGTDTWRD KWKEYYQPIR VTRYLTIVPQ WIEYEPQHPD
     EQLIVLDPGR SFGTGDHPTT RLTLHALEAT MLGGETVIDV GTGSGILSIA ARYLGAQQIV
     ASDVADEALA AAATNIALNG MTDDIVLEKR DLVHGLDLQA DIVVANILPE FLLPLIPQVH
     KNLRPTGKLI LSGIIMEKEN EIVTALNAAG FQVEEKITDG KWLALVAHNT LNS
//
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