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Database: UniProt
Entry: A0A368XBI5_9BACI
LinkDB: A0A368XBI5_9BACI
Original site: A0A368XBI5_9BACI 
ID   A0A368XBI5_9BACI        Unreviewed;       312 AA.
AC   A0A368XBI5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ORFNames=DFR57_11150 {ECO:0000313|EMBL:RCW65322.1};
OS   Saliterribacillus persicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Saliterribacillus.
OX   NCBI_TaxID=930114 {ECO:0000313|EMBL:RCW65322.1, ECO:0000313|Proteomes:UP000252585};
RN   [1] {ECO:0000313|EMBL:RCW65322.1, ECO:0000313|Proteomes:UP000252585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27696 {ECO:0000313|EMBL:RCW65322.1,
RC   ECO:0000313|Proteomes:UP000252585};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RCW65322.1}.
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DR   EMBL; QPJJ01000011; RCW65322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368XBI5; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000252585; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735,
KW   ECO:0000313|EMBL:RCW65322.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252585};
KW   Ribonucleoprotein {ECO:0000313|EMBL:RCW65322.1};
KW   Ribosomal protein {ECO:0000313|EMBL:RCW65322.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:RCW65322.1}.
FT   COILED          206..233
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         162
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         205
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   312 AA;  34653 MW;  B7A3DA9A817F1819 CRC64;
     MKWTELCIHT TNEAIEPISN IFHEAGASGV VIEDQSELDV QREDTYGEIY ELDPNDYPDE
     GVLLKAYLPV NSFLGETVAE IKQAINNLLL YDIDLGRNSI TLSEVNEEDW ATAWKKYYKP
     VKISERITIT PTWEDYQRVS SDELIIELDP GMAFGTGTHP TTVLSIQALE QYVKSNDTIL
     DVGCGSGVLS IASALLGAQE IFAYDLDEVA VKSAKLNAKV NKVEKKIHVK QNNLLNNVTT
     KADVIVANIL AEIILRFEKD AFSCLKSGGI FITSGIIQAK KDQVKSGLIN AGFEILEINQ
     MEDWISIIAR RP
//
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