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Database: UniProt
Entry: A0A143HGJ9_9BACL
LinkDB: A0A143HGJ9_9BACL
Original site: A0A143HGJ9_9BACL 
ID   A0A143HGJ9_9BACL        Unreviewed;       238 AA.
AC   A0A143HGJ9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_00074};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00074};
DE   AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
DE            Short=16S rRNA m7G methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
GN   Name=rsmG {ECO:0000256|HAMAP-Rule:MF_00074,
GN   ECO:0000313|EMBL:GEL06161.1};
GN   ORFNames=ATY39_15095 {ECO:0000313|EMBL:AMX00626.1}, RST01_27880
GN   {ECO:0000313|EMBL:GEL06161.1};
OS   Rummeliibacillus stabekisii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX   NCBI_TaxID=241244 {ECO:0000313|EMBL:AMX00626.1, ECO:0000313|Proteomes:UP000076021};
RN   [1] {ECO:0000313|EMBL:AMX00626.1, ECO:0000313|Proteomes:UP000076021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP9 {ECO:0000313|EMBL:AMX00626.1,
RC   ECO:0000313|Proteomes:UP000076021};
RX   PubMed=27231360;
RA   da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT   "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT   from Antarctic Soil.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000076021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:GEL06161.1, ECO:0000313|Proteomes:UP000321194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104870 {ECO:0000313|EMBL:GEL06161.1,
RC   ECO:0000313|Proteomes:UP000321194};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Rummeliibacillus stabekisii NBRC
RT   104870.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC       position 535 of 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC       methyltransferase RsmG family. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00074}.
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DR   EMBL; CP014806; AMX00626.1; -; Genomic_DNA.
DR   EMBL; BJVD01000010; GEL06161.1; -; Genomic_DNA.
DR   RefSeq; WP_066791191.1; NZ_JACHHC010000004.1.
DR   AlphaFoldDB; A0A143HGJ9; -.
DR   STRING; 241244.ATY39_15095; -.
DR   KEGG; rst:ATY39_15095; -.
DR   OrthoDB; 9808773at2; -.
DR   Proteomes; UP000076021; Chromosome.
DR   Proteomes; UP000321194; Unassembled WGS sequence.
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; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR   InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00138; rsmG_gidB; 1.
DR   PANTHER; PTHR31760; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR31760:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF02527; GidB; 1.
DR   PIRSF; PIRSF003078; GidB; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00074};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074,
KW   ECO:0000313|EMBL:AMX00626.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076021};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_00074}; S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00074};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00074, ECO:0000313|EMBL:AMX00626.1}.
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         82
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         128..129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   238 AA;  27217 MW;  661B10E4E37377C0 CRC64;
     MNEEQFMQSL KEQGIELSEK QVQQFHLYFE TLVEWNEKMN LTAITDQPSV YLKHFYDSIS
     AAFYINFNDI ESLCDVGAGA GFPSIPIKIC FPHLKVTIVD SLNKRIQFLH HLSDVLELEN
     MQFVHSRAED FGQMAQYREK FDLVTARAVA RLSVLSELCA PLVKNDGIFV AMKAASGEEE
     LTDAKKAIQV LGTKLMDQYK FSLPIENSER TIYVFKKIKS TPKKYPRKAG MPNKSPIH
//
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