PRMA_THET8
ID PRMA_THET8 Reviewed; 254 AA.
AC Q84BQ9; Q5SKI7;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305};
DE Short=L11 Mtase {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305|PubMed:15317787};
GN Name=prmA {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000303|PubMed:15317787};
GN OrderedLocusNames=TTHA0656;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION.
RX PubMed=12777815; DOI=10.1107/s0907444903004554;
RG RIKEN structural genomics initiative (RSGI);
RT "Crystallization and preliminary X-ray diffraction analysis of ribosomal
RT protein L11 methyltransferase from Thermus thermophilus HB8.";
RL Acta Crystallogr. D 59:930-932(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15317787; DOI=10.1128/jb.186.17.5819-5825.2004;
RA Cameron D.M., Gregory S.T., Thompson J., Suh M.-J., Limbach P.A.,
RA Dahlberg A.E.;
RT "Thermus thermophilus L11 methyltransferase, PrmA, is dispensable for
RT growth and preferentially modifies free ribosomal protein L11 prior to
RT ribosome assembly.";
RL J. Bacteriol. 186:5819-5825(2004).
RN [4] {ECO:0007744|PDB:1UFK}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-254.
RA Kaminishi T., Sakai H., Takemoto-Hori C., Terada T., Nakagawa N., Maoka N.,
RA Kuramitsu S., Shirouzu M., Yokoyama S.;
RT "Crystal structure of TT0836.";
RL Submitted (NOV-2003) to the PDB data bank.
RN [5] {ECO:0007744|PDB:2NXC, ECO:0007744|PDB:2NXE, ECO:0007744|PDB:2NXJ, ECO:0007744|PDB:2NXN}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP S-ADENOSYL-L-METHIONINE AND RIBOSOMAL PROTEIN L11, AND DOMAIN.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=17215866; DOI=10.1038/sj.emboj.7601508;
RA Demirci H., Gregory S.T., Dahlberg A.E., Jogl G.;
RT "Recognition of ribosomal protein L11 by the protein trimethyltransferase
RT PrmA.";
RL EMBO J. 26:567-577(2007).
RN [6] {ECO:0007744|PDB:2ZBP, ECO:0007744|PDB:2ZBQ, ECO:0007744|PDB:2ZBR}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEXES WITH
RP S-ADENOSYL-L-METHIONINE; S-ADENOSYL-L-HOMOCYSTEINE AND
RP S-ADENOSYL-ORNITHINE.
RA Kaminishi T., Sakai H., Takemoto-Hori C., Terada T., Nakagawa N., Maoka N.,
RA Kuramitsu S., Shirouzu M., Yokoyama S.;
RT "Crystal structure of ribosomal protein L11 methyltransferase from Thermus
RT thermophilus.";
RL Submitted (OCT-2007) to the PDB data bank.
RN [7] {ECO:0007744|PDB:3CJQ, ECO:0007744|PDB:3CJR, ECO:0007744|PDB:3CJS, ECO:0007744|PDB:3CJT, ECO:0007744|PDB:3EGV}
RP X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 1-59 IN COMPLEXES WITH
RP S-ADENOSYL-L-METHIONINE; S-ADENOSYL-L-HOMOCYSTEINE AND RIBOSOMAL PROTEIN
RP L11, AND DOMAIN.
RX PubMed=18611379; DOI=10.1016/j.str.2008.03.016;
RA Demirci H., Gregory S.T., Dahlberg A.E., Jogl G.;
RT "Multiple-site trimethylation of ribosomal protein L11 by the PrmA
RT methyltransferase.";
RL Structure 16:1059-1066(2008).
CC -!- FUNCTION: Methylates ribosomal protein L11 (PubMed:15317787).
CC Preferentially recognizes free L11 before its incorporation into 50S
CC subunits (PubMed:15317787). This function is dispensable for growth and
CC thermostability (PubMed:15317787). {ECO:0000269|PubMed:15317787}.
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, ECO:0000305|PubMed:15317787};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-terminal L-alpha-aminoacyl-[protein] + 3 S-adenosyl-L-
CC methionine = an N-terminal trimethyl-L-alpha-aminoacyl-[protein] + 3
CC H(+) + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62916, Rhea:RHEA-
CC COMP:10636, Rhea:RHEA-COMP:16230, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:78597,
CC ChEBI:CHEBI:146135; Evidence={ECO:0000305|PubMed:15317787};
CC -!- INTERACTION:
CC Q84BQ9; P36238: rplK; Xeno; NbExp=2; IntAct=EBI-7202232, EBI-15714407;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00735}.
CC -!- DOMAIN: Contains an N-terminal substrate recognition domain and a C-
CC terminal methyltransferase domain, connected by a flexible linker.
CC {ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379}.
CC -!- DISRUPTION PHENOTYPE: Mutant contains unmethylated protein L11
CC (PubMed:15317787). Null mutant is perfectly viable (PubMed:15317787).
CC {ECO:0000269|PubMed:15317787}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305}.
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DR EMBL; AB103400; BAC67244.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70479.1; -; Genomic_DNA.
DR RefSeq; WP_011228100.1; NC_006461.1.
DR RefSeq; YP_143922.1; NC_006461.1.
DR PDB; 1UFK; X-ray; 1.90 A; A=1-254.
DR PDB; 2NXC; X-ray; 1.59 A; A=1-254.
DR PDB; 2NXE; X-ray; 1.75 A; A/B=1-254.
DR PDB; 2NXJ; X-ray; 2.30 A; A/B=1-254.
DR PDB; 2NXN; X-ray; 2.40 A; A=1-254.
DR PDB; 2ZBP; X-ray; 2.30 A; A=1-254.
DR PDB; 2ZBQ; X-ray; 2.40 A; A=1-254.
DR PDB; 2ZBR; X-ray; 1.90 A; A=1-254.
DR PDB; 3CJQ; X-ray; 2.70 A; A/D/G=1-254.
DR PDB; 3CJR; X-ray; 2.05 A; A=1-254.
DR PDB; 3CJS; X-ray; 1.37 A; A=1-59.
DR PDB; 3CJT; X-ray; 2.30 A; A/C/E/G/I/K/M/O=1-254.
DR PDB; 3EGV; X-ray; 1.75 A; A=1-254.
DR PDBsum; 1UFK; -.
DR PDBsum; 2NXC; -.
DR PDBsum; 2NXE; -.
DR PDBsum; 2NXJ; -.
DR PDBsum; 2NXN; -.
DR PDBsum; 2ZBP; -.
DR PDBsum; 2ZBQ; -.
DR PDBsum; 2ZBR; -.
DR PDBsum; 3CJQ; -.
DR PDBsum; 3CJR; -.
DR PDBsum; 3CJS; -.
DR PDBsum; 3CJT; -.
DR PDBsum; 3EGV; -.
DR AlphaFoldDB; Q84BQ9; -.
DR SMR; Q84BQ9; -.
DR DIP; DIP-44643N; -.
DR IntAct; Q84BQ9; 2.
DR MINT; Q84BQ9; -.
DR STRING; 300852.55772038; -.
DR EnsemblBacteria; BAD70479; BAD70479; BAD70479.
DR GeneID; 3168879; -.
DR KEGG; ttj:TTHA0656; -.
DR PATRIC; fig|300852.9.peg.650; -.
DR eggNOG; COG2264; Bacteria.
DR HOGENOM; CLU_049382_3_1_0; -.
DR OMA; EFFFIFP; -.
DR PhylomeDB; Q84BQ9; -.
DR BRENDA; 2.1.1.244; 2305.
DR EvolutionaryTrace; Q84BQ9; -.
DR Proteomes; UP000000532; 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 SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..254
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_0000192328"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735,
FT ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379,
FT ECO:0000269|Ref.6"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735,
FT ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379,
FT ECO:0000269|Ref.6"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735,
FT ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379,
FT ECO:0000269|Ref.6"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:17215866,
FT ECO:0000269|PubMed:18611379, ECO:0000269|Ref.6"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735,
FT ECO:0000269|PubMed:17215866, ECO:0000269|PubMed:18611379,
FT ECO:0000269|Ref.6"
FT CONFLICT 225
FT /note="P -> S (in Ref. 1; BAC67244)"
FT /evidence="ECO:0000305"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3CJS"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:3CJS"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3CJS"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:3CJS"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:3CJS"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3CJS"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3CJS"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2NXE"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2NXC"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:2NXC"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2NXC"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2NXC"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2NXC"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:2NXC"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 208..220
FT /evidence="ECO:0007829|PDB:2NXC"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2NXC"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:2NXC"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:2NXC"
SQ SEQUENCE 254 AA; 27631 MW; D33A79573F360946 CRC64;
MWVYRLKGTL EALDPILPGL FDGGARGLWE REGEVWAFFP APVDLPYEGV WEEVGDEDWL
EAWRRDLKPA LAPPFVVLAP WHTWEGAEIP LVIEPGMAFG TGHHETTRLA LKALARHLRP
GDKVLDLGTG SGVLAIAAEK LGGKALGVDI DPMVLPQAEA NAKRNGVRPR FLEGSLEAAL
PFGPFDLLVA NLYAELHAAL APRYREALVP GGRALLTGIL KDRAPLVREA MAGAGFRPLE
EAAEGEWVLL AYGR
