PRMA_HELPH
ID PRMA_HELPH Reviewed; 329 AA.
AC Q1CUC6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00735};
DE Short=L11 Mtase {ECO:0000255|HAMAP-Rule:MF_00735};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00735};
GN Name=prmA {ECO:0000255|HAMAP-Rule:MF_00735}; OrderedLocusNames=HPAG1_0379;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00735};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00735}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000255|HAMAP-Rule:MF_00735}.
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DR EMBL; CP000241; ABF84446.1; -; Genomic_DNA.
DR RefSeq; WP_000917415.1; NC_008086.1.
DR AlphaFoldDB; Q1CUC6; -.
DR SMR; Q1CUC6; -.
DR EnsemblBacteria; ABF84446; ABF84446; HPAG1_0379.
DR KEGG; hpa:HPAG1_0379; -.
DR HOGENOM; CLU_049382_1_0_7; -.
DR OMA; EFFFIFP; -.
DR OrthoDB; 1712450at2; -.
DR Proteomes; UP000008835; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00735; Methyltr_PrmA; 1.
DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF000401; RPL11_MTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00406; prmA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..329
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_1000192635"
FT BINDING 177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 264
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ SEQUENCE 329 AA; 37780 MW; 65FE79CAB46AAC7A CRC64;
MLKPMYYEFF FIFPKERELF ESFLLDTTHL ALEESSLENL KAFDDKETIE FISQSSWHYF
ATHDPLKEHL KEKPQHLKNF VILRSQKDLN NSLILALEAF CLNLKQNLQS EFDFFYLSRN
LASKDWLEAY KQAILPVQCA KFYIHPSWHQ KPSHISTDDC IMIDPALAFG SGHHESTSMC
LELLSDLDLK RKNALDVGCG SGILSIALKK QGVSALVACD TDSLAVEETL KNFSLNQIPL
LAQDKVIYGS TQKIEGRFDI IVANLVADVV KSLYSEFVRL CNHTLILSGI LETHLNSVLQ
IYYNGFEILE QRQRNEWVAL KLLKKQPIN
