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Protein

Ribosomal RNA small subunit methyltransferase C

Gene

rsmC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.

Catalytic activityi

S-adenosyl-L-methionine + guanine(1207) in 16S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(1207) in 16S rRNA.

Cofactori

GO - Molecular functioni

  • 16S rRNA (guanine(1207)-N(2))-methyltransferase activity Source: EcoCyc
  • nucleic acid binding Source: InterPro
  • rRNA (guanine-N2-)-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • rRNA base methylation Source: EcoCyc
  • rRNA methylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

Magnesium, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:G7950-MONOMER.
ECOL316407:JW4333-MONOMER.
MetaCyc:G7950-MONOMER.
BRENDAi2.1.1.172. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal RNA small subunit methyltransferase C (EC:2.1.1.172)
Alternative name(s):
16S rRNA m2G1207 methyltransferase
rRNA (guanine-N(2)-)-methyltransferase RsmC
Gene namesi
Name:rsmC
Synonyms:yjjT
Ordered Locus Names:b4371, JW4333
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12596. rsmC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861K → S: Reduces activity by 84%; when associated with S-88. 1 Publication
Mutagenesisi88 – 881K → S: Reduces activity by 84%; when associated with S-86. 1 Publication
Mutagenesisi202 – 2021D → A: Abolishes affinity for S-adenosyl-L-methionine. Loss of activity. 1 Publication
Mutagenesisi227 – 2271D → A: Strongly reduces affinity for S-adenosyl-L-methionine. Reduces activity by 87%. 1 Publication
Mutagenesisi268 – 2681N → A: Reduces affinity for S-adenosyl-L-methionine. Reduces activity by 80%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 343342Ribosomal RNA small subunit methyltransferase CPRO_0000097490Add
BLAST

Proteomic databases

EPDiP39406.
PaxDbiP39406.
PRIDEiP39406.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4262778. 9 interactions.
DIPiDIP-10804N.
IntActiP39406. 14 interactions.
STRINGi511145.b4371.

Structurei

Secondary structure

1
343
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127Combined sources
Helixi15 – 184Combined sources
Beta strandi22 – 276Combined sources
Helixi33 – 364Combined sources
Beta strandi40 – 489Combined sources
Helixi49 – 5911Combined sources
Helixi60 – 623Combined sources
Beta strandi63 – 653Combined sources
Helixi71 – 744Combined sources
Beta strandi78 – 836Combined sources
Helixi88 – 9912Combined sources
Beta strandi107 – 1137Combined sources
Helixi114 – 1163Combined sources
Helixi118 – 1203Combined sources
Helixi121 – 1255Combined sources
Turni126 – 1283Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi140 – 1467Combined sources
Helixi155 – 1584Combined sources
Beta strandi160 – 1645Combined sources
Beta strandi167 – 1715Combined sources
Beta strandi178 – 1803Combined sources
Helixi183 – 1919Combined sources
Helixi209 – 2179Combined sources
Beta strandi224 – 2296Combined sources
Helixi230 – 24213Combined sources
Beta strandi248 – 2514Combined sources
Turni254 – 2574Combined sources
Beta strandi262 – 2676Combined sources
Beta strandi273 – 2753Combined sources
Helixi276 – 28914Combined sources
Helixi290 – 2923Combined sources
Beta strandi293 – 30412Combined sources
Helixi309 – 3179Combined sources
Beta strandi321 – 3255Combined sources
Beta strandi327 – 3359Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PJDX-ray2.10A1-343[»]
ProteinModelPortaliP39406.
SMRiP39406. Positions 3-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39406.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D8J. Bacteria.
COG2813. LUCA.
HOGENOMiHOG000218308.
InParanoidiP39406.
KOiK00564.
OMAiRHCQLWQ.
OrthoDBiEOG67X1ZC.
PhylomeDBiP39406.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01862. 16SrRNA_methyltr_C.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR013675. Mtase_sm_N.
IPR023543. rRNA_ssu_MeTfrase_C.
IPR029063. SAM-dependent_MTases.
IPR007848. Small_mtfrase_dom.
[Graphical view]
PfamiPF05175. MTS. 1 hit.
PF08468. MTS_N. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAFTPASEV LLRHSDDFEQ SRILFAGDLQ DDLPARLDTA ASRAHTQQFH
60 70 80 90 100
HWQVLSRQMG DNARFSLVAT ADDVADCDTL IYYWPKNKPE AQFQLMNLLS
110 120 130 140 150
LLPVGTDIFV VGENRSGVRS AEQMLADYAP LNKVDSARRC GLYFGRLEKQ
160 170 180 190 200
PVFDAEKFWG EYSVDGLTVK TLPGVFSRDG LDVGSQLLLS TLTPHTKGKV
210 220 230 240 250
LDVGCGAGVL SVAFARHSPK IRLTLCDVSA PAVEASRATL AANGVEGEVF
260 270 280 290 300
ASNVFSEVKG RFDMIISNPP FHDGMQTSLD AAQTLIRGAV RHLNSGGELR
310 320 330 340
IVANAFLPYP DVLDETFGFH EVIAQTGRFK VYRAIMTRQA KKG
Length:343
Mass (Da):37,625
Last modified:January 23, 2007 - v3
Checksum:i81E190CB86E4BAC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97267.1.
U00096 Genomic DNA. Translation: AAC77324.1.
AP009048 Genomic DNA. Translation: BAE78359.1.
PIRiS56595.
RefSeqiNP_418788.1. NC_000913.3.
WP_001272330.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77324; AAC77324; b4371.
BAE78359; BAE78359; BAE78359.
GeneIDi948892.
KEGGiecj:JW4333.
eco:b4371.
PATRICi32124352. VBIEscCol129921_4516.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97267.1.
U00096 Genomic DNA. Translation: AAC77324.1.
AP009048 Genomic DNA. Translation: BAE78359.1.
PIRiS56595.
RefSeqiNP_418788.1. NC_000913.3.
WP_001272330.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PJDX-ray2.10A1-343[»]
ProteinModelPortaliP39406.
SMRiP39406. Positions 3-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262778. 9 interactions.
DIPiDIP-10804N.
IntActiP39406. 14 interactions.
STRINGi511145.b4371.

Proteomic databases

EPDiP39406.
PaxDbiP39406.
PRIDEiP39406.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77324; AAC77324; b4371.
BAE78359; BAE78359; BAE78359.
GeneIDi948892.
KEGGiecj:JW4333.
eco:b4371.
PATRICi32124352. VBIEscCol129921_4516.

Organism-specific databases

EchoBASEiEB2481.
EcoGeneiEG12596. rsmC.

Phylogenomic databases

eggNOGiENOG4105D8J. Bacteria.
COG2813. LUCA.
HOGENOMiHOG000218308.
InParanoidiP39406.
KOiK00564.
OMAiRHCQLWQ.
OrthoDBiEOG67X1ZC.
PhylomeDBiP39406.

Enzyme and pathway databases

BioCyciEcoCyc:G7950-MONOMER.
ECOL316407:JW4333-MONOMER.
MetaCyc:G7950-MONOMER.
BRENDAi2.1.1.172. 2026.

Miscellaneous databases

EvolutionaryTraceiP39406.
PROiP39406.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01862. 16SrRNA_methyltr_C.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR013675. Mtase_sm_N.
IPR023543. rRNA_ssu_MeTfrase_C.
IPR029063. SAM-dependent_MTases.
IPR007848. Small_mtfrase_dom.
[Graphical view]
PfamiPF05175. MTS. 1 hit.
PF08468. MTS_N. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Purification, cloning, and characterization of the 16S RNA m2G1207 methyltransferase from Escherichia coli."
    Tscherne J.S., Nurse K., Popienick P., Ofengand J.
    J. Biol. Chem. 274:924-929(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20, CHARACTERIZATION.
  5. "Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC."
    Sunita S., Purta E., Durawa M., Tkaczuk K.L., Swaathi J., Bujnicki J.M., Sivaraman J.
    Nucleic Acids Res. 35:4264-4274(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF LYS-86; LYS-88; ASP-202; ASP-227 AND ASN-268, SUBUNIT.

Entry informationi

Entry nameiRSMC_ECOLI
AccessioniPrimary (citable) accession number: P39406
Secondary accession number(s): Q2M5U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.