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Database: UniProt
Entry: B6I202
LinkDB: B6I202
Original site: B6I202 
ID   RSMB_ECOSE              Reviewed;         429 AA.
AC   B6I202;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   01-OCT-2014, entry version 43.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000255|HAMAP-Rule:MF_01856};
DE            EC=2.1.1.176 {ECO:0000255|HAMAP-Rule:MF_01856};
DE   AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01856};
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000255|HAMAP-Rule:MF_01856};
GN   Name=rsmB {ECO:0000255|HAMAP-Rule:MF_01856};
GN   Synonyms=sun {ECO:0000255|HAMAP-Rule:MF_01856};
GN   OrderedLocusNames=ECSE_3563;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H.,
RA   Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy
RT   adult.";
RL   DNA Res. 15:375-386(2008).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967
CC       (m5C967) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01856}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(967) in 16S
CC       rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_01856}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01856}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000255|HAMAP-Rule:MF_01856}.
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DR   EMBL; AP009240; BAG79087.1; -; Genomic_DNA.
DR   RefSeq; YP_002294838.1; NC_011415.1.
DR   ProteinModelPortal; B6I202; -.
DR   SMR; B6I202; 5-428.
DR   STRING; 409438.ECSE_3563; -.
DR   EnsemblBacteria; BAG79087; BAG79087; ECSE_3563.
DR   GeneID; 7001948; -.
DR   KEGG; ecy:ECSE_3563; -.
DR   PATRIC; 18425756; VBIEscCol83070_3731.
DR   eggNOG; COG0144; -.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; GHDGFYY; -.
DR   OrthoDB; EOG6091D0; -.
DR   BioCyc; ECOL409438:GHUU-3629-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01856; 16SrRNA_methyltr_B; 1.
DR   InterPro; IPR001678; Fmu/NOL1/Nop2p.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR023541; rRNA_ssu_MeTfrase_B_ent.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   Pfam; PF01189; Nol1_Nop2_Fmu; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; SSF48013; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00563; rsmB; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    429       Ribosomal RNA small subunit
FT                                methyltransferase B.
FT                                /FTId=PRO_1000188695.
FT   REGION      254    260       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01856}.
FT   ACT_SITE    375    375       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01856}.
FT   BINDING     277    277       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01856}.
FT   BINDING     303    303       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01856}.
FT   BINDING     322    322       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01856}.
SQ   SEQUENCE   429 AA;  48319 MW;  D84166307B4D80F2 CRC64;
     MKKQRNLRSM AAQAVEQVVE QGQSLSNILP PLQQKVSDKD KALLQELCFG VLRTLSQLDW
     LINKLMARPM TGKQRTVHYL IMVGLYQLLY TRIPPHAALA ETVEGAIAIK RPQLKGLING
     VLRQFQRQQE ELLAEFNASD ARYLHPSWLL KRLQKAYPEQ WQSIVEANNQ RPPMWLRVNR
     THHSRDSWLA LLDEAGMKGF PHADYPDAVR LETPAPVHAL PGFEDGWVTV QDASAQGCMT
     WLAPQNGEHI LDLCAAPGGK TTHILEVAPE AQVVAVDIDE QRLSRVYDNL KRLGMKATVK
     QGDGRYPSQW CGEQQFDRIL LDAPCSATGV IRRHPDIKWL RRDRDIPELA QLQSEILDAI
     WPHLKSGGTL VYATCSVLPE ENSLQIKAFL QRTADAELCE TGTPEQPGKQ NLPGAEEGDG
     FFYAKLIKK
//
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