RSMJ_ECO57
ID RSMJ_ECO57 Reviewed; 250 AA.
AC P68568; P37633; P76707;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_01523};
DE EC=2.1.1.242 {ECO:0000255|HAMAP-Rule:MF_01523};
DE AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
GN Name=rsmJ {ECO:0000255|HAMAP-Rule:MF_01523}; Synonyms=yhiQ;
GN OrderedLocusNames=Z4897, ECs4369;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of UPF0341 protein YhiQ from Escherichia coli.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Specifically methylates the guanosine in position 1516 of 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43220, Rhea:RHEA-COMP:10412, Rhea:RHEA-COMP:10413,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.242;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01523};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01523}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family.
CC {ECO:0000255|HAMAP-Rule:MF_01523}.
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; AE005174; AAG58629.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37792.1; -; Genomic_DNA.
DR PIR; A86021; A86021.
DR PIR; A98175; A98175.
DR RefSeq; NP_312396.1; NC_002695.1.
DR RefSeq; WP_000686620.1; NZ_SWKA01000005.1.
DR PDB; 2PGX; X-ray; 2.00 A; A=1-250.
DR PDBsum; 2PGX; -.
DR AlphaFoldDB; P68568; -.
DR SMR; P68568; -.
DR STRING; 155864.EDL933_4735; -.
DR EnsemblBacteria; AAG58629; AAG58629; Z4897.
DR EnsemblBacteria; BAB37792; BAB37792; ECs_4369.
DR GeneID; 58461299; -.
DR GeneID; 915773; -.
DR KEGG; ece:Z4897; -.
DR KEGG; ecs:ECs_4369; -.
DR PATRIC; fig|386585.9.peg.4563; -.
DR eggNOG; COG0742; Bacteria.
DR HOGENOM; CLU_076324_0_0_6; -.
DR OMA; SRYDIYP; -.
DR BRENDA; 2.1.1.242; 2026.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01523; 16SrRNA_methyltr_J; 1.
DR InterPro; IPR007536; 16SrRNA_methylTrfase_J.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR36112; PTHR36112; 1.
DR Pfam; PF04445; SAM_MT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..250
FT /note="Ribosomal RNA small subunit methyltransferase J"
FT /id="PRO_0000212065"
FT BINDING 101..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 117..118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 153..154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:2PGX"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2PGX"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:2PGX"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2PGX"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:2PGX"
SQ SEQUENCE 250 AA; 26949 MW; 628C4329BAC1C97C CRC64;
MKICLIDETG TGDGALSVLA ARWGLEHDED NLMALVLTPE HLELRKRDEP KLGGIFVDFV
GGAMAHRRKF GGGRGEAVAK AVGIKGDYLP DVVDATAGLG RDAFVLASVG CRVRMLERNP
VVAALLDDGL ARGYADAEIG GWLQERLQLI HASSLTALTD ITPRPQVVYL DPMFPHKQKS
ALVKKEMRVF QSLVGPDLDA DGLLEPARLL ATKRVVVKRP DYAPPLANVA TPNAVVTKGH
RFDIYAGTPV