GenomeNet

Database: UniProt/TrEMBL
Entry: C4X0Q5_KLEPN
LinkDB: C4X0Q5_KLEPN
Original site: C4X0Q5_KLEPN 
ID   C4X0Q5_KLEPN            Unreviewed;       431 AA.
AC   C4X0Q5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   26-NOV-2014, entry version 41.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000256|HAMAP-Rule:MF_01856, ECO:0000256|SAAS:SAAS00029844};
DE            EC=2.1.1.176 {ECO:0000256|HAMAP-Rule:MF_01856, ECO:0000256|SAAS:SAAS00029845};
DE   AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01856};
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|HAMAP-Rule:MF_01856};
GN   Name=rrmB {ECO:0000313|EMBL:BAH65463.1};
GN   Synonyms=rsmB {ECO:0000256|HAMAP-Rule:MF_01856}, sun
GN   {ECO:0000256|HAMAP-Rule:MF_01856};
GN   ORFNames=KP1_5007 {ECO:0000313|EMBL:BAH65463.1};
OS   Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=484021 {ECO:0000313|EMBL:BAH65463.1, ECO:0000313|Proteomes:UP000010106};
RN   [1] {ECO:0000313|EMBL:BAH65463.1, ECO:0000313|Proteomes:UP000010106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTUH-K2044 {ECO:0000313|EMBL:BAH65463.1};
RX   PubMed=19447910; DOI=10.1128/JB.00315-09;
RA   Wu K.-M., Li L.-H., Yan J.-J., Tsao N., Liao T.-L., Tsai H.-C.,
RA   Fung C.-P., Chen H.-J., Liu Y.-M., Wang J.-T., Fang C.-T.,
RA   Chang S.-C., Shu H.-Y., Liu T.-T., Chen Y.-T., Shiau Y.-R.,
RA   Lauderdale T.-L., Su I.-J., Kirby R., Tsai S.-F.;
RT   "Genome sequencing and comparative analysis of Klebsiella pneumoniae
RT   NTUH-K2044, a strain causing liver abscess and meningitis.";
RL   J. Bacteriol. 191:4492-4501(2009).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967
CC       (m5C967) of 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_01856,
CC       ECO:0000256|SAAS:SAAS00029818}.
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:0000256|HAMAP-Rule:MF_01856,
CC       ECO:0000256|SAAS:SAAS00029823}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01856,
CC       ECO:0000256|SAAS:SAAS00029836}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|HAMAP-Rule:MF_01856}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP006725; BAH65463.1; -; Genomic_DNA.
DR   RefSeq; YP_002921530.1; NC_012731.1.
DR   ProteinModelPortal; C4X0Q5; -.
DR   STRING; 484021.KP1_5007; -.
DR   EnsemblBacteria; BAH65463; BAH65463; KP1_5007.
DR   GeneID; 7947380; -.
DR   KEGG; kpu:KP1_5007; -.
DR   PATRIC; 20453247; VBIKlePne21779_4392.
DR   eggNOG; COG0144; -.
DR   KO; K03500; -.
DR   OrthoDB; EOG6091D0; -.
DR   BioCyc; KPNE484021:GCWL-4650-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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000010106};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|SAAS:SAAS00029858};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|SAAS:SAAS00029830};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|SAAS:SAAS00029827};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|SAAS:SAAS00149471};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|SAAS:SAAS00029840};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|SAAS:SAAS00029849}.
FT   REGION      254    260       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01856}.
FT   ACT_SITE    375    375       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01856}.
FT   BINDING     277    277       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01856}.
FT   BINDING     303    303       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01856}.
FT   BINDING     322    322       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01856}.
SQ   SEQUENCE   431 AA;  48617 MW;  2FD4A202B124BD33 CRC64;
     MKKNINLRSL AAQAIEQVVE KGQSLSNVLP PLQQKVSDKD KALLQELCFG VLRTLSQLEW
     LISKLMARPM TGKQRTVHFL IMVGLYQLLY TRIPPHAALA ETVEGAVAIK RPQLKGLING
     VLRQFQRQQE ALLAEFAEHE NRYLHPKWLL KRLQQAWPQQ WQEIVEANNQ RPPMWLRVNR
     NHHSRDEWLA LLNETGLEGF THPDYPDAVR LATPAPVHAL PGFAEGWVTV QDASAQGCMR
     YLQPENGERI LDLCAAPGGK TTHILEVAPQ AQVMAVDIDE QRLSRVYDNL KRLGVKAEVK
     QGDGRFPEQW CGNEQFDRIL LDAPCSATGV IRRHPDIKWL RRDRDIAELA QLQAEILNAT
     WTHLKPGGTL VYATCSILPE ENSQQIAAFL ARTPDAELHA TGTPASPGQQ NLPGVEEGDG
     FFYAKLIKRR N
//
DBGET integrated database retrieval system