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Database: UniProt
Entry: C6XHX8_LIBAP
LinkDB: C6XHX8_LIBAP
Original site: C6XHX8_LIBAP 
ID   C6XHX8_LIBAP            Unreviewed;       284 AA.
AC   C6XHX8;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
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:ACT56871.1};
GN   OrderedLocusNames=CLIBASIA_01415 {ECO:0000313|EMBL:ACT56871.1};
OS   Liberibacter asiaticus (strain psy62).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=537021 {ECO:0000313|EMBL:ACT56871.1, ECO:0000313|Proteomes:UP000002744};
RN   [1] {ECO:0000313|EMBL:ACT56871.1, ECO:0000313|Proteomes:UP000002744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX   PubMed=19589076; DOI=10.1094/MPMI-22-8-1011;
RA   Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L.,
RA   Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y.,
RA   Gottwald T.;
RT   "Complete genome sequence of citrus huanglongbing bacterium, 'Candidatus
RT   Liberibacter asiaticus' obtained through metagenomics.";
RL   Mol. Plant Microbe Interact. 22:1011-1020(2009).
RN   [2] {ECO:0000313|EMBL:ACT56871.1, ECO:0000313|Proteomes:UP000002744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX   PubMed=21784907; DOI=10.1128/AEM.05111-11;
RA   Zhou L., Powell C.A., Hoffman M.T., Li W., Fan G., Liu B., Lin H., Duan Y.;
RT   "Diversity and plasticity of the intracellular plant pathogen and insect
RT   symbiont, 'Candidatus Liberibacter asiaticus', revealed by hyper variable
RT   prophage genes with intragenic tandem repeats.";
RL   Appl. Environ. Microbiol. 77:6663-6673(2011).
CC   -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and
CC       A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA
CC       in the 30S particle. May play a critical role in biogenesis of 30S
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00607}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-
CC         methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-
CC         dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:19609, Rhea:RHEA-COMP:10232, Rhea:RHEA-COMP:10233,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.182;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00607};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00607}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family. RsmA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00607}.
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DR   EMBL; CP001677; ACT56871.1; -; Genomic_DNA.
DR   RefSeq; WP_012778617.1; NC_012985.3.
DR   AlphaFoldDB; C6XHX8; -.
DR   STRING; 537021.CLIBASIA_01415; -.
DR   GeneID; 66285865; -.
DR   KEGG; las:CLIBASIA_01415; -.
DR   eggNOG; COG0030; Bacteria.
DR   HOGENOM; CLU_041220_0_1_5; -.
DR   OrthoDB; 9814755at2; -.
DR   Proteomes; UP000002744; 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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like_C.
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_sf.
DR   NCBIfam; TIGR00755; ksgA; 1.
DR   PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00607};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00607};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00607};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_00607};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00607};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00607}.
FT   DOMAIN          35..212
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         28
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT                   ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         30
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT                   ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT                   ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT                   ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT                   ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00607,
FT                   ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   284 AA;  32281 MW;  BA3DA7E7EA11BFEB CRC64;
     MTMNNKSHSL KTILSHYKII PKKYMGQNFL LDLNILKKIA ESSGSLDGIT VIEIGAGPGN
     LTQMLLTLGA RKVIVIEKDQ QFFPILKDIS SQHPNRLEII QDDALKVDFE KFFNISSPIR
     IIANLPYNIG TRLLFNWISA DTWPPFWESL TLLFQKEVGE RITAQKNSPH YGRLSVLTGW
     RTKATMMFDI SPHVFFPSPK VTSTVIHFIP HLNPIPCCLE SLKKITQEAF GKRRKTLRQS
     LKRLGGENLL HQAGIETNLR AENLSIEDFC RITNILTDNQ DIAI
//
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