(data stored in ACNUC10821 zone)

SWISSPROT: C8U1C4_ECO10

ID   C8U1C4_ECO10            Unreviewed;       273 AA.
AC   C8U1C4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000256|HAMAP-Rule:MF_00607};
DE            EC=2.1.1.182 {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethylase {ECO:0000256|HAMAP-Rule:MF_00607};
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000256|HAMAP-Rule:MF_00607};
GN   Name=rsmA {ECO:0000256|HAMAP-Rule:MF_00607};
GN   Synonyms=ksgA {ECO:0000256|HAMAP-Rule:MF_00607,
GN   ECO:0000313|EMBL:BAI28932.1};
GN   OrderedLocusNames=ECO103_0054 {ECO:0000313|EMBL:BAI28932.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28932.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28932.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518
CC       and A1519) in the loop of a conserved hairpin near the 3'-end of
CC       16S rRNA in the 30S particle. May play a critical role in
CC       biogenesis of 30S subunits. {ECO:0000256|HAMAP-Rule:MF_00607}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-
CC         adenosyl-L-methionine = 4 H(+) + N(6)-
CC         dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA
CC         + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19609, Rhea:RHEA-
CC         COMP:10232, Rhea:RHEA-COMP:10233, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74493; EC=2.1.1.182; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00607};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
CC       ECO:0000256|SAAS:SAAS00344807}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. rRNA adenine N(6)-methyltransferase
CC       family. RsmA subfamily. {ECO:0000256|HAMAP-Rule:MF_00607,
CC       ECO:0000256|SAAS:SAAS00540765}.
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DR   EMBL; AP010958; BAI28932.1; -; Genomic_DNA.
DR   RefSeq; WP_001065381.1; NC_013353.1.
DR   SMR; C8U1C4; -.
DR   EnsemblBacteria; BAI28932; BAI28932; ECO103_0054.
DR   KEGG; eoh:ECO103_0054; -.
DR   HOGENOM; HOG000227962; -.
DR   KO; K02528; -.
DR   OMA; KRFGQHW; -.
DR   BioCyc; ECOL585395:ECO103_RS00275-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.100; -; 1.
DR   HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR11727; PTHR11727; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00755; ksgA; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1C4.
DR   SWISS-2DPAGE; C8U1C4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00423242};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314909,
KW   ECO:0000313|EMBL:BAI28932.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314905};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|SAAS:SAAS00445489};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00607,
KW   ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|SAAS:SAAS00423218};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00607, ECO:0000256|PROSITE-
KW   ProRule:PRU01026, ECO:0000256|SAAS:SAAS00314911,
KW   ECO:0000313|EMBL:BAI28932.1}.
FT   DOMAIN       25    198       rADc. {ECO:0000259|SMART:SM00650}.
FT   BINDING      18     18       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      20     20       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00607, ECO:0000256|PROSITE-ProRule:
FT                                PRU01026}.
FT   BINDING      45     45       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      66     66       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING      91     91       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
FT   BINDING     113    113       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00607,
FT                                ECO:0000256|PROSITE-ProRule:PRU01026}.
SQ   SEQUENCE   273 AA;  30420 MW;  BBB163A0F4011C9D CRC64;
     MNNRVHQGHL ARKRFGQNFL NDQFVIDSIV SAINPQKGQA MVEIGPGLAA LTEPVGERLD
     QLTVIELDRD LAARLQTHPF LGPKLTIYQQ DAMTFNFGEL AEKMGQPLRV FGNLPYNIST
     PLMFHLFSYT DAIADMHFML QKEVVNRLVA GPNSKAYGRL SVMAQYYCNV IPVLEVPPSA
     FTPPPKVDSA VVRLVPHATM PHPVKDVRVL SRITTEAFNQ RRKTIRNSLG NLFSVEVLTG
     MGIDPAMRAE NISVAQYCQM ANYLAENAPL QES
//

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