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Database: UniProt
Entry: A0A0U5KZ89_9GAMM
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ID   A0A0U5KZ89_9GAMM        Unreviewed;       347 AA.
AC   A0A0U5KZ89;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase C {ECO:0000256|HAMAP-Rule:MF_01862};
DE            EC=2.1.1.172 {ECO:0000256|HAMAP-Rule:MF_01862};
DE   AltName: Full=16S rRNA m2G1207 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01862};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RsmC {ECO:0000256|HAMAP-Rule:MF_01862};
GN   Name=yjjT {ECO:0000313|EMBL:CUU22863.1};
GN   Synonyms=rsmC {ECO:0000256|HAMAP-Rule:MF_01862};
GN   ORFNames=EM595_0626 {ECO:0000313|EMBL:CUU22863.1};
OS   Duffyella gerundensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Duffyella.
OX   NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU22863.1, ECO:0000313|Proteomes:UP000059419};
RN   [1] {ECO:0000313|Proteomes:UP000059419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Blom J.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the guanine in position 1207 of 16S
CC       rRNA in the 30S particle. {ECO:0000256|HAMAP-Rule:MF_01862}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42736, Rhea:RHEA-COMP:10213, Rhea:RHEA-COMP:10214,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.172;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01862};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01862}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01862}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmC family.
CC       {ECO:0000256|HAMAP-Rule:MF_01862}.
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DR   EMBL; LN907827; CUU22863.1; -; Genomic_DNA.
DR   RefSeq; WP_067427785.1; NZ_LN907827.1.
DR   AlphaFoldDB; A0A0U5KZ89; -.
DR   STRING; 1619313.EM595_0626; -.
DR   KEGG; ege:EM595_0626; -.
DR   PATRIC; fig|1619313.3.peg.654; -.
DR   OrthoDB; 9816072at2; -.
DR   Proteomes; UP000059419; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052914; F:16S rRNA (guanine(1207)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   HAMAP; MF_01862; 16SrRNA_methyltr_C; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR013675; Mtase_sm_N.
DR   InterPro; IPR023543; rRNA_ssu_MeTfrase_C.
DR   InterPro; IPR046977; RsmC/RlmG.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   PANTHER; PTHR47816; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR   PANTHER; PTHR47816:SF4; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF08468; MTS_N; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01862};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01862,
KW   ECO:0000313|EMBL:CUU22863.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01862};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01862};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01862, ECO:0000313|EMBL:CUU22863.1}.
FT   DOMAIN          8..162
FT                   /note="Methyltransferase small N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08468"
FT   DOMAIN          167..333
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
SQ   SEQUENCE   347 AA;  37944 MW;  7DB792BBD765E650 CRC64;
     MPAFSPASEV ILRHSDEFTE RRVLFAGDLQ DDLPAQLETQ LSKVFTQQYH HWQLLSPRLE
     ENARFSLVAT ADDVSDCDTL VYYWPKSKPE AQYQLQNLLS LLPEGCDLFV IGENRSGVRS
     AEGMVEAWAK LDKIDSARRC GLYHGKLETR PDFDAESFWH SYEVDGLTIK TLPGVFSRDG
     LDAGSRLLLS TLSAHTKGKV LDVGCGAGVL SATLASHSPK VRLTLTDVNA AAVAASKATL
     AANQLEGEVF PSNVFSDVTG RFDMIISNPP FHEGTQTSLD AAQTLIRGAA KHLNTGGELR
     IVANAFLPYA QVLDETFGSH EVLAQTGRFK VYRAVYGRAA KALRSAK
//
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