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Entry: A0A3A9K6K7_9BACI
LinkDB: A0A3A9K6K7_9BACI
Original site: A0A3A9K6K7_9BACI 
ID   A0A3A9K6K7_9BACI        Unreviewed;       313 AA.
AC   A0A3A9K6K7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=CR203_01020 {ECO:0000313|EMBL:RKL68664.1};
OS   Salipaludibacillus neizhouensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=885475 {ECO:0000313|EMBL:RKL68664.1, ECO:0000313|Proteomes:UP000281498};
RN   [1] {ECO:0000313|EMBL:RKL68664.1, ECO:0000313|Proteomes:UP000281498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13187 {ECO:0000313|EMBL:RKL68664.1,
RC   ECO:0000313|Proteomes:UP000281498};
RA   Wang H.;
RT   "Bacillus sp. nov., a halophilic bacterium isolated from a Keqin Lake.";
RL   Submitted (OCT-2017) 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:RKL68664.1}.
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DR   EMBL; PDOE01000001; RKL68664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9K6K7; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000281498; 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:RKL68664.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281498};
KW   Ribonucleoprotein {ECO:0000313|EMBL:RKL68664.1};
KW   Ribosomal protein {ECO:0000313|EMBL:RKL68664.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:RKL68664.1}.
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   313 AA;  34412 MW;  D00138A47FEB2689 CRC64;
     MKWSEISIQT SQEAVDPVSN ILHEAGASGV VIEDPEDLKR DWETKFGEIY ELSPDDYPEE
     GVLLKAYLPV NSFLGDAVDE IKEAINQLLA YNIDIGHNKV TVSEVNEEDW ATAWKKYYKP
     VKISDHITIT PTWEDYKAVQ DDEMIIELDP GMAFGTGTHP TTVLCIQALE KHMKKGSTVV
     DVGTGSGVLS IAAAKLGAAR VEALDLDEVA VESALLNITL NNTQDIVSVQ QSNLLDQVKD
     SSDIIVANIL AEVVVKMTKD AFRLLEPNGK LITSGIIQTK RAMVKEAMLS AGFQIDEIVE
     MEDWIAIVAK KPE
//
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