PRMA_HELPY
ID PRMA_HELPY Reviewed; 333 AA.
AC O07678;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 119.
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}; Synonyms=hsm;
GN OrderedLocusNames=HP_1068;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=9244252; DOI=10.1128/jb.179.15.4676-4683.1997;
RA Beier D., Spohn G., Rappuoli R., Scarlato V.;
RT "Identification and characterization of an operon of Helicobacter pylori
RT that is involved in motility and stress adaptation.";
RL J. Bacteriol. 179:4676-4683(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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, ECO:0000305}.
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DR EMBL; U97567; AAB66376.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD08114.1; -; Genomic_DNA.
DR PIR; D64653; D64653.
DR RefSeq; NP_207859.1; NC_000915.1.
DR RefSeq; WP_000917395.1; NC_018939.1.
DR AlphaFoldDB; O07678; -.
DR SMR; O07678; -.
DR DIP; DIP-3670N; -.
DR IntAct; O07678; 2.
DR MINT; O07678; -.
DR STRING; 85962.C694_05520; -.
DR PaxDb; O07678; -.
DR EnsemblBacteria; AAD08114; AAD08114; HP_1068.
DR KEGG; hpy:HP_1068; -.
DR PATRIC; fig|85962.47.peg.1147; -.
DR eggNOG; COG2264; Bacteria.
DR OMA; EFFFIFP; -.
DR PhylomeDB; O07678; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..333
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_0000192269"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT VARIANT 22
FT /note="S -> N (in strain: NCTC 11638)"
FT VARIANT 27
FT /note="A -> T (in strain: NCTC 11638)"
FT VARIANT 50
FT /note="G -> E (in strain: NCTC 11638)"
FT VARIANT 61
FT /note="A -> T (in strain: NCTC 11638)"
FT VARIANT 65
FT /note="P -> S (in strain: NCTC 11638)"
FT VARIANT 78
FT /note="P -> S (in strain: NCTC 11638)"
FT VARIANT 90..92
FT /note="QKD -> EEN (in strain: NCTC 11638)"
FT VARIANT 99
FT /note="P -> L (in strain: NCTC 11638)"
FT VARIANT 107
FT /note="N -> S (in strain: NCTC 11638)"
FT VARIANT 109
FT /note="K -> Q (in strain: NCTC 11638)"
FT VARIANT 144
FT /note="T -> A (in strain: NCTC 11638)"
FT VARIANT 190..191
FT /note="DI -> NL (in strain: NCTC 11638)"
FT VARIANT 251
FT /note="I -> V (in strain: NCTC 11638)"
FT VARIANT 317
FT /note="Q -> K (in strain: NCTC 11638)"
SQ SEQUENCE 333 AA; 38160 MW; 92E2B9F221F827AF CRC64;
MLKPMYYEFF FIFPKERELF ESFLLDATHL ALEESSLENL KAFDDKETIG FISQSNWHYF
ATHDPLKKDL KENLKEKPPH LKNFVILRSQ KDLNNSLIPA LEAFCLNLKQ NLQSEFDFFY
LSRNLASKDW LEAYKQAILP VQCTKFYIHP SWHQKPSHVV TNDCIMIDPA LAFGSGHHES
TSMCLELLSD IDLKRKNALD VGCGSGILSI ALKKQGVSAL VACDTDSLAV EETLKNFSLN
QIPLLVQDKV IYGSTQKIEG RFDVIVANLV ADVIKSLYSE FVRLCNHTLI LSGILETHLN
SVLQIYYNGF EVLEQRQRNE WVALKLLKKQ PIN
