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Database: UniProt/SWISS-PROT
Entry: RSMB_YERPA
LinkDB: RSMB_YERPA
Original site: RSMB_YERPA 
ID   RSMB_YERPA              Reviewed;         429 AA.
AC   Q1C2X7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   01-OCT-2014, entry version 62.
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=YPA_3233;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG15195.1; -; Genomic_DNA.
DR   RefSeq; YP_653140.1; NC_008150.1.
DR   ProteinModelPortal; Q1C2X7; -.
DR   SMR; Q1C2X7; 6-428.
DR   STRING; 360102.YPA_3233; -.
DR   PRIDE; Q1C2X7; -.
DR   EnsemblBacteria; ABG15195; ABG15195; YPA_3233.
DR   GeneID; 4118502; -.
DR   KEGG; ypa:YPA_3233; -.
DR   PATRIC; 18586318; VBIYerPes1796_3954.
DR   eggNOG; COG0144; -.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; GHDGFYY; -.
DR   OrthoDB; EOG6091D0; -.
DR   BioCyc; YPES360102:GHZU-3303-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_0000366185.
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;  48444 MW;  0E18231A62D8782E CRC64;
     MKNTYNLRSI AAKAISQVLD QGQSLSAVLP ELQKNISDKD RALLQELCFG TLRVLPQLEW
     CIQQLMARPM TGKQRVFHYL IMVGLYQLIY TRIPPHAALA ETVEGATVLK RPQLKGLING
     VLRQFQRQQV ELLERAVNND SHYLHPSWLL ARIKQAYPAQ WQQILDANNQ RPPMWLRVNR
     LHHSRSEYLE LLTQADINAE PHPIYRDAVR LITPCAVNHL PGFELGWVTV QDASAQGCVD
     LLDPQNGEQI LDLCAAPGGK TTHILEAAPK AHVLAVDIDE QRLSRVKENL QRLQLQAVVR
     VGDGRAPDTW CGDQQFDRIL LDAPCSATGV IRRHPDIKWL RRDRDISELA QLQSEIIEAI
     WPKLKHGGVL VYATCSILPE ENQQQIAAFL QRHPEAQLTE TGTTAAPGKQ NLPHPEDGDG
     FFYAKIIKK
//
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