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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}.
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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
 
 
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