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Protein

rRNA adenine N-6-methyltransferase

Gene

ermC'

Organism
Bacillus subtilis
Status
Reviewed-Annotation score: -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

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

Catalytic activityi

2 S-adenosyl-L-methionine + adenine(2085) in 23S rRNA = 2 S-adenosyl-L-homocysteine + N6-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

Keywordsi

Molecular functionMethyltransferase, RNA-binding, Transferase
Biological processAntibiotic resistance
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.184 658
SABIO-RKiP13956

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
DrugBankiDB01752 S-Adenosyl-L-Homocysteine
DB01910 Sinefungin

PTM / Processingi

Molecule processing

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

Proteomic databases

PRIDEiP13956

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, 2 hits
InterProiView protein in InterPro
IPR001737 KsgA/Erm
IPR023165 rRNA_Ade_diMease-like
IPR020596 rRNA_Ade_Mease_Trfase_CS
IPR020598 rRNA_Ade_methylase_Trfase_N
IPR029063 SAM-dependent_MTases
PANTHERiPTHR11727 PTHR11727, 1 hit
PfamiView protein in Pfam
PF00398 RrnaAD, 1 hit
SMARTiView protein in SMART
SM00650 rADc, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS01131 RRNA_A_DIMETH, 1 hit
PS51689 SAM_RNA_A_N6_MT, 1 hit

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
31596600
KEGGiag:AAA98136

Similar proteinsi

Entry informationi

Entry nameiERM_BACIU
AccessioniPrimary (citable) accession number: P13956
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 23, 2018
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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
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Main funding by: National Institutes of Health