ID   PRMA_CLOAB              Reviewed;         311 AA.
AC   P45558; Q9ZIA3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 3.
DT   03-AUG-2022, entry version 117.
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=CA_C1284;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-298.
RX   PubMed=7507453; DOI=10.1016/0378-1097(93)90141-n;
RA   Behrens S., Narberhaus F., Bahl H.;
RT   "Cloning, nucleotide sequence and structural analysis of the Clostridium
RT   acetobutylicum dnaJ gene.";
RL   FEMS Microbiol. Lett. 114:53-60(1993).
RN   [3]
RP   SEQUENCE REVISION.
RA   Behrens S.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-311.
RC   STRAIN=ATCC 4259 / DSM 1731 / NCIB 619;
RA   Jacobi C.S.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC       {ECO:0000255|HAMAP-Rule:MF_00735, ECO:0000305}.
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; AE001437; AAK79255.1; -; Genomic_DNA.
DR   EMBL; X69050; CAA48793.1; -; Genomic_DNA.
DR   EMBL; AF036764; AAD02056.1; -; Genomic_DNA.
DR   PIR; D97058; D97058.
DR   RefSeq; NP_347915.1; NC_003030.1.
DR   RefSeq; WP_010964596.1; NC_003030.1.
DR   AlphaFoldDB; P45558; -.
DR   SMR; P45558; -.
DR   STRING; 272562.CA_C1284; -.
DR   EnsemblBacteria; AAK79255; AAK79255; CA_C1284.
DR   GeneID; 44997790; -.
DR   KEGG; cac:CA_C1284; -.
DR   PATRIC; fig|272562.8.peg.1485; -.
DR   eggNOG; COG2264; Bacteria.
DR   HOGENOM; CLU_049382_0_1_9; -.
DR   OMA; EFFFIFP; -.
DR   OrthoDB; 1712450at2; -.
DR   Proteomes; UP000000814; 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   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Stress response; Transferase.
FT   CHAIN           1..311
FT                   /note="Ribosomal protein L11 methyltransferase"
FT                   /id="PRO_0000192252"
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"
SQ   SEQUENCE   311 AA;  35028 MW;  2D71786B3C974922 CRC64;
     MDKDWFEVSV ITSSEAVEAV TGILYNTPVK GVAIEDSKDV EFKKKHPGDW DYFDESLLNV
     KDGAVIKAYY KDDHNFDESV KYIEESIDKL SEFGINKGEG KVFVNKVNET DWENNWKKYY
     KPTKIGARIV VKPLWEEYTP KDYELMLNMD PGMAFGTGTH ETTRMCIQAL ERYVNEDAEV
     FDIGTGSGIL AIAAAKLNAK KVLGVDLDSV AVKAAKENIQ YNNVNNIEIL HGNLMEVVQG
     KADIIVANII ADVINILIPD INKFLKTDGY FISSGIIKDR AEDVIENLKK NKFEIIEVNN
     QGEWICIVAK L