PRMA_LACDB
ID PRMA_LACDB Reviewed; 314 AA.
AC Q04AV7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=LBUL_0809;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=321956;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-365 / Lb-18;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN [2] {ECO:0007744|PDB:3GRZ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 117-313.
RC STRAIN=ATCC BAA-365 / Lb-18;
RA Patskovsky Y., Ramagopal U.A., Toro R., Morano C., Freeman J., Chang S.,
RA Sauder J.M., Burley S.K., Almo S.C.;
RT "Crystal structure of ribosomal protein 11 methylase from Lactobacillus
RT delbrueckii subsp. bulgaricus.";
RL Submitted (MAR-2009) to the PDB data bank.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000412; ABJ58415.1; -; Genomic_DNA.
DR RefSeq; WP_011678185.1; NC_008529.1.
DR PDB; 3GRZ; X-ray; 2.00 A; A/B=117-313.
DR PDBsum; 3GRZ; -.
DR AlphaFoldDB; Q04AV7; -.
DR SMR; Q04AV7; -.
DR KEGG; lbu:LBUL_0809; -.
DR HOGENOM; CLU_049382_0_1_9; -.
DR OMA; EFFFIFP; -.
DR BioCyc; LDEL321956:LBUL_RS03850-MON; -.
DR EvolutionaryTrace; Q04AV7; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..314
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_1000062124"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 184
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3GRZ"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3GRZ"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:3GRZ"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3GRZ"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:3GRZ"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3GRZ"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3GRZ"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 265..277
FT /evidence="ECO:0007829|PDB:3GRZ"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3GRZ"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:3GRZ"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:3GRZ"
SQ SEQUENCE 314 AA; 34931 MW; B3B8E6080241F65F CRC64;
MKLLEIKIES SYDVEDALAY FATEDLKALG TEARRRSDFE QAGWLHDSTV VDMDDIPNLP
DELEFIAYFD EETDPEEMVK CFKDKLAELA GYGLKTAPGE ISVDYVADQD WNTVWKKYYH
VINLSRHLAI VPEWEDYQPV FKDQEIIRLD PGLAFGTGNH QTTQLAMLGI ERAMVKPLTV
ADVGTGSGIL AIAAHKLGAK SVLATDISDE SMTAAEENAA LNGIYDIALQ KTSLLADVDG
KFDLIVANIL AEILLDLIPQ LDSHLNEDGQ VIFSGIDYLQ LPKIEQALAE NSFQIDLKMR
AGRWIGLAIS RKHD
