(data stored in ACNUC29543 zone)

SWISSPROT: RSMJ_ACIBT

ID   RSMJ_ACIBT              Reviewed;         279 AA.
AC   A3M2K0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAY-2019, entry version 61.
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};
GN   OrderedLocusNames=A1S_0700;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: Specifically methylates the guanosine in position 1516
CC       of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine =
CC         H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:43220, Rhea:RHEA-COMP:10412,
CC         Rhea:RHEA-COMP:10413, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74481;
CC         EC=2.1.1.242; 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
CC       family. {ECO:0000255|HAMAP-Rule:MF_01523}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABO11144.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; CP000521; ABO11144.2; ALT_INIT; Genomic_DNA.
DR   SMR; A3M2K0; -.
DR   EnsemblBacteria; ABO11144; ABO11144; A1S_0700.
DR   KEGG; acb:A1S_0700; -.
DR   HOGENOM; HOG000218236; -.
DR   KO; K15984; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01523; 16SrRNA_methyltr_J; 1.
DR   InterPro; IPR007536; 16SrRNA_methylTrfase_J.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR36112; PTHR36112; 1.
DR   Pfam; PF04445; SAM_MT; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
DR   PRODOM; A3M2K0.
DR   SWISS-2DPAGE; A3M2K0.
KW   Cytoplasm; Methyltransferase; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    279       Ribosomal RNA small subunit
FT                                methyltransferase J.
FT                                /FTId=PRO_0000296963.
FT   REGION      138    139       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01523}.
FT   BINDING     194    194       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01523}.
SQ   SEQUENCE   279 AA;  31978 MW;  A640B50BB0EB80D7 CRC64;
     MEKNCGSGQS KLKALRMHIY FEVDFQEQAQ HYQAVLYSRG VTVDLQPIEK LNARFLRLNP
     DLALCVDENG LWLSANGMKM QPDWKAEIPR LKRATLKSEM IARACQLGEK PVLVDATAGL
     GHDSLLMAYL GAQIQLVERH PILFTLLEDS KAQAQHDPFL SQFMDRIQLI FADSASYLQQ
     LDQEEKTVDV VYLDPMFPQR DQNQQAIKKQ AQVKKQMQLL HLLLPEDGEM DLGDHLLELA
     KKVAKRVIVK RPRHAIFLAN QEPAHQWQGD ACRFDAYFQ
//

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