ID U2FUA6_9GAMM Unreviewed; 299 AA.
AC U2FUA6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:ERJ17953.1};
GN ORFNames=SSPSH_003172 {ECO:0000313|EMBL:ERJ17953.1};
OS Salinisphaera shabanensis E1L3A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ17953.1, ECO:0000313|Proteomes:UP000006242};
RN [1] {ECO:0000313|EMBL:ERJ17953.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ17953.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=21705588; DOI=10.1128/JB.05459-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT the harsh, variable environment of the brine-seawater interface of the
RT Shaban Deep in the Red Sea.";
RL J. Bacteriol. 193:4555-4556(2011).
RN [2] {ECO:0000313|EMBL:ERJ17953.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ17953.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(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:ERJ17953.1}.
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DR EMBL; AFNV02000025; ERJ17953.1; -; Genomic_DNA.
DR RefSeq; WP_006915366.1; NZ_AFNV02000025.1.
DR AlphaFoldDB; U2FUA6; -.
DR STRING; 1033802.SSPSH_003172; -.
DR eggNOG; COG2264; Bacteria.
DR OrthoDB; 9785995at2; -.
DR Proteomes; UP000006242; 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:ERJ17953.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006242};
KW Ribonucleoprotein {ECO:0000313|EMBL:ERJ17953.1};
KW Ribosomal protein {ECO:0000313|EMBL:ERJ17953.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:ERJ17953.1}.
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ SEQUENCE 299 AA; 32039 MW; E962E2C175B2711E CRC64;
MAETRSPVAW LQITVETPKA SLAEAVFESF DAEAVTVLDA GDDITVENTP NEQPAFQDSR
ITGLFTDGTR AEPIETALRD ALGDEAVIRV DRLENEDWAS AWLAQHPPIR FGERLWIAPH
NAPVEADDDA IIVRLDPGLA FGTGTHPTTA LCLEWLATAD LAGKDVLDYG CGSGILAVAA
ARLGAASVTA VDIDDQAVRA TQENAERNGV LDRIHTPPLD DIGEREFDIV LANILAKPLI
ALAPTLTAHA APGAPLVLSG LLTRQIEDVK NAYTRAFEFA EPVVEEDWVC LNGRRHGAG
//
