ID Card:
Full name:
rRNA adenine N-6-methyltransferase
GI:
127199
COG:
COG0030
UniProt:
P10738
Alpha Fold Predicted Structure:
AF-P10738-F1
Enzyme type:
methyltransferase
Position of modification - modification:
l :2058(2058) - m6A
Protein sequence:
MNKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKSNTRVTLIHQDILQFQFPNKQRYKIVGNIPYHLSTQIIKKVVFESHASDIYLIVEEGFYKRTLDIHRTLGLLLHTQVSIQQLLKLPAECFHPKPRVNSVLIKLTRHTTDVPDKYWKLYTYFVSKWVNREYRQLFTKNQFHQAMKHAKVNNLSTVTYEQVLSIFNSYLLFNGRK
Comments:
ErmBC methylates the exocyclic amine of A2058 in the Peptidyl Center (between helix 73 and 74) of 23S rRNA. It is responsible for the development of bacterial resistance to lincosamide/ Streptogramin-type of antibiotics. This enzyme arose in E. coli by lateral gene transfer from a gram-positive bacteria Brisson-Noël et al. 1988 ).
Reaction
Substrate
SubstrateType
Position
(Anti)Codon
Modified (Anti)Codon
Amino Acid Change
Transcript Name
Transcript Region
Cellular Localization
References
A:m6A
RNA
rRNA
2058
LSU - 23S
exocyclic amine of A2058 in Peptidyl Center between helix 73 and 74
Prokaryotic Cytosol
2832378
Alpha Fold Predicted Structure:
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Protein sequence:
M
N
K
N
I
K
Y
S
Q
N
F
L
T
S
E
K
V
L
N
Q
I
I
K
Q
L
N
L
K
E
T
D
T
V
Y
E
I
G
T
G
K
G
H
L
T
T
K
L
A
K
I
S
K
Q
V
T
S
I
E
L
D
S
H
L
F
N
L
S
S
E
K
L
K
S
N
T
R
V
T
L
I
H
Q
D
I
L
Q
F
Q
F
P
N
K
Q
R
Y
K
I
V
G
N
I
P
Y
H
L
S
T
Q
I
I
K
K
V
V
F
E
S
H
A
S
D
I
Y
L
I
V
E
E
G
F
Y
K
R
T
L
D
I
H
R
T
L
G
L
L
L
H
T
Q
V
S
I
Q
Q
L
L
K
L
P
A
E
C
F
H
P
K
P
R
V
N
S
V
L
I
K
L
T
R
H
T
T
D
V
P
D
K
Y
W
K
L
Y
T
Y
F
V
S
K
W
V
N
R
E
Y
R
Q
L
F
T
K
N
Q
F
H
Q
A
M
K
H
A
K
V
N
N
L
S
T
V
T
Y
E
Q
V
L
S
I
F
N
S
Y
L
L
F
N
G
R
K
Secondary Structure Alphabet
G: 3-turn helix (310 helix) H: α-helix I: 𝝅-helix (5 - turn helix) T: Hydrogen Bonded Turn B: β-sheet S: Bend C: Coil (residues not present in any of the above conformations) N: Not assigned
Download PDB Structures & DSSP Secondary Structures:
Publications:
Title
Authors
Journal
Details
PubMed Id DOI
Evidence for natural gene transfer from gram-positive cocci to Escherichia coli.
Brisson-Noel A, Arthur M, Courvalin P
J Bacteriol
[details]
2832378
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Links: