ID   RLMKL_ACIBC             Reviewed;         734 AA.
AC   B2HWX8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase K/L {ECO:0000255|HAMAP-Rule:MF_01858};
DE   Includes:
DE     RecName: Full=23S rRNA m2G2445 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01858};
DE              EC=2.1.1.173 {ECO:0000255|HAMAP-Rule:MF_01858};
DE     AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmL {ECO:0000255|HAMAP-Rule:MF_01858};
DE   Includes:
DE     RecName: Full=23S rRNA m7G2069 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01858};
DE              EC=2.1.1.264 {ECO:0000255|HAMAP-Rule:MF_01858};
DE     AltName: Full=rRNA (guanine-N(7)-)-methyltransferase RlmK {ECO:0000255|HAMAP-Rule:MF_01858};
GN   Name=rlmL {ECO:0000255|HAMAP-Rule:MF_01858}; OrderedLocusNames=ACICU_01168;
OS   Acinetobacter baumannii (strain ACICU).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=405416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACICU;
RX   PubMed=18411315; DOI=10.1128/aac.01643-07;
RA   Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA   Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT   "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT   Acinetobacter baumannii strain belonging to the European clone II group.";
RL   Antimicrob. Agents Chemother. 52:2616-2625(2008).
CC   -!- FUNCTION: Specifically methylates the guanine in position 2445
CC       (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01858}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42740, Rhea:RHEA-COMP:10215, Rhea:RHEA-COMP:10216,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.173;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01858};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2069) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(2069) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43772, Rhea:RHEA-COMP:10688, Rhea:RHEA-COMP:10689,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.264;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01858};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01858}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmKL family.
CC       {ECO:0000255|HAMAP-Rule:MF_01858}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACC56480.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000863; ACC56480.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001098013.1; NC_010611.1.
DR   AlphaFoldDB; B2HWX8; -.
DR   SMR; B2HWX8; -.
DR   KEGG; abc:ACICU_01168; -.
DR   HOGENOM; CLU_014042_2_0_6; -.
DR   Proteomes; UP000008839; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052915; F:23S rRNA (guanine(2445)-N(2))-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 2.
DR   HAMAP; MF_01858; 23SrRNA_methyltr_KL; 1.
DR   InterPro; IPR017244; 23SrRNA_methyltr_KL.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR000241; RNA_methylase_dom.
DR   InterPro; IPR019614; SAM-dep_methyl-trfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR004114; THUMP_dom.
DR   Pfam; PF10672; Methyltrans_SAM; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   Pfam; PF01170; UPF0020; 1.
DR   PIRSF; PIRSF037618; RNA_Mtase_bacteria_prd; 1.
DR   SMART; SM00981; THUMP; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS51165; THUMP; 1.
DR   PROSITE; PS01261; UPF0020; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..734
FT                   /note="Ribosomal RNA large subunit methyltransferase K/L"
FT                   /id="PRO_0000366714"
FT   DOMAIN          49..167
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ   SEQUENCE   734 AA;  83873 MW;  4DFAAE534577BBAB CRC64;
     MNTSLRLNHY WITCADGLET LLQEEIEQLG TKVTERKAGR LIIEGTLEHA YRICMWSRLA
     SRVLLPIHTY ELERTHDARD VAEELYEGAI SFDWSLIFAP QSTFAIRLHA EREIKVNTQF
     ATLRVKDGVV DSFMEAVGRR PSIDTKQPEI TLYVLAGKTE HTYCLDLSGD SLHKRGYRRF
     MTDAPIKENL AAAILQKAKL KERNPEIVLD PMCGSGTFII EALMILTDRA PGLVRRFGFN
     GWHGHDRELW LSLKAEAAER HEKALEQPLP KFYAYDADWE AVKATRENII AAGFEKLLGD
     IQIEERTLAD WPDFGAENKT AFIVTNPPYG ERLGDKASNR SLYLGLSALL QKNFPNQYAA
     IIAAQIEQAD VLAFEAPETL RLMNGKLPIY VRFGTVKPEK VTQPFLANWQ AQPVEMEEAQ
     DFANRLQKNM TALKKWATKE NIYCLRLYDA DLPDFNLAVD LYGDRLHVQE YAPPKKIDPE
     KAKKRFNLAL AAIRAVTGLN RDAIFIKTRA RQTGTNQYTK QSTANKRFIV QEGKAKILVN
     LTDYLDTGLF LDHRQMRLRI AKEARGKHFL NLYSYTSTAS LHAALGGAAS TTSVDLSNTY
     LSWSKENFVL NGLTVDHADE QHMFFASDCF EWLKEGHEQY DLIFIDPPTF SNSKKFHGTF
     DVQRDHVSLI KRAMNRLTSE GTLYFSNNYR GFEMDEEIEA LYEVEEITSE TIGPDFKRNQ
     KIHRAWKIQH PGLN