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Protein

rRNA adenine N-6-methyltransferase

Gene

ermC'

Organism
Bacillus subtilis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.2 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + adenine(2085) in 23S rRNA = 2 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(2085) in 23S rRNA.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei11S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei13S-adenosyl-L-methionine; via amide nitrogen1
Binding sitei38S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei59S-adenosyl-L-methionine1
Binding sitei84S-adenosyl-L-methionine1
Binding sitei101S-adenosyl-L-methionine1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.184. 658.
SABIO-RKP13956.

Names & Taxonomyi

Protein namesi
Recommended name:
rRNA adenine N-6-methyltransferase (EC:2.1.1.184)
Alternative name(s):
Erythromycin resistance protein
Macrolide-lincosamide-streptogramin B resistance protein
Gene namesi
Name:ermC'
Encoded oniPlasmid pIM130 Publication
OrganismiBacillus subtilis
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11N → A: Reduces activity about 3-fold. 1
Mutagenesisi101N → A: Decreases affinity for S-adenosyl-L-methionine 4-fold. Reduces activity by 90%. 1 Publication1
Mutagenesisi104Y → A: Loss of activity. 1 Publication1
Mutagenesisi108T → A: Decreases affinity for S-adenosyl-L-methionine 8-fold. Reduces activity by 99%. 1 Publication1
Mutagenesisi112R → A: Reduces activity by 90%. 1 Publication1
Mutagenesisi112R → D: Decreases affinity for S-adenosyl-L-methionine 5-fold. Decreases affinity for RNA 6-fold. Reduces activity by 99%. 1 Publication1
Mutagenesisi133K → A: Reduces activity by about 80%. 1 Publication1
Mutagenesisi134R → A: Decreases affinity for S-adenosyl-L-methionine 7-fold. Decreases affinity for RNA about 4-fold. Reduces activity by over 99%. May severely impair protein folding. 1 Publication1
Mutagenesisi140R → A: Decreases affinity for S-adenosyl-L-methionine 7-fold. Reduces activity by about 85%. 1 Publication1
Mutagenesisi165P → A: Decreases affinity for S-adenosyl-L-methionine 6-fold. Reduces activity by about 96%. 1 Publication1
Mutagenesisi166K → A: Decreases affinity for RNA about 6-fold. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001016741 – 244rRNA adenine N-6-methyltransferaseAdd BLAST244

Interactioni

Chemistry databases

BindingDBiP13956.

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 23Combined sources8
Beta strandi33 – 37Combined sources5
Helixi43 – 51Combined sources9
Beta strandi52 – 58Combined sources7
Helixi62 – 71Combined sources10
Turni72 – 74Combined sources3
Beta strandi77 – 81Combined sources5
Helixi85 – 87Combined sources3
Beta strandi92 – 94Combined sources3
Beta strandi97 – 101Combined sources5
Helixi104 – 106Combined sources3
Helixi107 – 116Combined sources10
Beta strandi121 – 128Combined sources8
Helixi129 – 135Combined sources7
Beta strandi138 – 140Combined sources3
Helixi141 – 146Combined sources6
Turni147 – 149Combined sources3
Beta strandi150 – 158Combined sources9
Helixi160 – 162Combined sources3
Beta strandi163 – 165Combined sources3
Beta strandi171 – 178Combined sources8
Helixi185 – 187Combined sources3
Helixi188 – 199Combined sources12
Helixi203 – 205Combined sources3
Helixi209 – 219Combined sources11
Helixi229 – 242Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QAMX-ray2.20A1-244[»]
1QANX-ray2.40A1-244[»]
1QAOX-ray2.70A1-244[»]
1QAQX-ray2.80A1-244[»]
2ERCX-ray3.03A/B1-244[»]
ProteinModelPortaliP13956.
SMRiP13956.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13956.

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

KOiK00561.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13956-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEKNIKHSQ NFITSKHNID KIMTNIRLNE HDNIFEIGSG KGHFTLELVQ
60 70 80 90 100
RCNFVTAIEI DHKLCKTTEN KLVDHDNFQV LNKDILQFKF PKNQSYKIFG
110 120 130 140 150
NIPYNISTDI IRKIVFDSIA DEIYLIVEYG FAKRLLNTKR SLALFLMAEV
160 170 180 190 200
DISILSMVPR EYFHPKPKVN SSLIRLNRKK SRISHKDKQK YNYFVMKWVN
210 220 230 240
KEYKKIFTKN QFNNSLKHAG IDDLNNISFE QFLSLFNSYK LFNK
Length:244
Mass (Da):28,907
Last modified:January 1, 1990 - v1
Checksum:iFC7CA6524034D820
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13761 Genomic DNA. Translation: AAA98136.1.
PIRiB25233.
RefSeqiNP_040407.1. NC_001376.1.
WP_001003263.1. NG_047806.1.

Genome annotation databases

GeneIDi1263203.
KEGGiag:AAA98136.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13761 Genomic DNA. Translation: AAA98136.1.
PIRiB25233.
RefSeqiNP_040407.1. NC_001376.1.
WP_001003263.1. NG_047806.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QAMX-ray2.20A1-244[»]
1QANX-ray2.40A1-244[»]
1QAOX-ray2.70A1-244[»]
1QAQX-ray2.80A1-244[»]
2ERCX-ray3.03A/B1-244[»]
ProteinModelPortaliP13956.
SMRiP13956.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP13956.
ChEMBLiCHEMBL4251.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1263203.
KEGGiag:AAA98136.

Phylogenomic databases

KOiK00561.

Enzyme and pathway databases

BRENDAi2.1.1.184. 658.
SABIO-RKP13956.

Miscellaneous databases

EvolutionaryTraceiP13956.
PROiP13956.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERM_BACIU
AccessioniPrimary (citable) accession number: P13956
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

In the genome of Neisseria meningitidis (serogroup B), the gene for this protein is present (NMB0066). It was introduced as part of a construct built to neutralize the virulence of the bacterium.Curated

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.