RSMG_MYCPA
ID RSMG_MYCPA Reviewed; 248 AA.
AC Q9L7M3;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00074};
DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE AltName: Full=Glucose-inhibited division protein B;
GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; Synonyms=gidB;
GN OrderedLocusNames=MAP_4345c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-245.
RA Zhang Q., Kapur V.;
RT "Genomic organization of the Mycobacterium avium subsp. paratuberculosis
RT origin of replication region.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC position 518 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}.
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DR EMBL; AE016958; AAS06895.1; -; Genomic_DNA.
DR EMBL; AF222789; AAF33688.1; -; Genomic_DNA.
DR RefSeq; WP_003874364.1; NC_002944.2.
DR AlphaFoldDB; Q9L7M3; -.
DR SMR; Q9L7M3; -.
DR STRING; 262316.MAP_4345c; -.
DR EnsemblBacteria; AAS06895; AAS06895; MAP_4345c.
DR KEGG; mpa:MAP_4345c; -.
DR PATRIC; fig|262316.17.peg.4624; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_5_0_11; -.
DR OMA; WDRHVLN; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31760; PTHR31760; 1.
DR Pfam; PF02527; GidB; 1.
DR PIRSF; PIRSF003078; GidB; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00138; rsmG_gidB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..248
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000184282"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 143..144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ SEQUENCE 248 AA; 26593 MW; 4FA13F748E13E811 CRC64;
MFHVKHVGPV EPAAGDPEVP PVAELGAAPE SAAALFGPRL ATAQRYAEVL GTAGVERGLL
GPREVDRIWD RHILNSAAVA ELLGRGDRII DIGSGAGLPG IPLAIARPDL EVVLLEPLLR
RSEFLTEVVD ELGLAVEVVR GRAEERPVRD RFGERDAAVS RAVAALDKLT KWSMPLLRHD
GRMLAIKGER AAEEVDRYRR VMTASGAADV RVVTCGANYL RPPATVVSAR RAKPPHPKSA
RTGKAGTR