ID   KAMB_STRHI              Reviewed;         215 AA.
AC   Q2MEY3;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=16S rRNA (adenine(1408)-N(1))-methyltransferase;
DE            EC=2.1.1.180;
DE   AltName: Full=16S rRNA m1A1408 methyltransferase;
GN   Name=kamB; ORFNames=ShinN01.6;
OS   Streptoalloteichus hindustanus.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Streptoalloteichus.
OX   NCBI_TaxID=2017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 44523;
RA   Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Comparison of the 'mixed' gene clusters for the biosynthesis of the
RT   aminoglycoside antibiotics apramycin (Streptoalloteichus hindustanus DSM
RT   44523 and Streptomyces tenebrarius DSM 40477) and hygromycin B
RT   (Streptomyces hygroscopicus subsp. hygroscopicus DSM 40578), which contain
RT   genes related to both the biosynthesis of other aminoglycosides and cell-
RT   wall sugars.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   3D-STRUCTURE MODELING, AND IDENTIFICATION OF START SITE.
RX   PubMed=17495534; DOI=10.4161/cc.6.10.4231;
RA   Koscinski L., Feder M., Bujnicki J.M.;
RT   "Identification of a missing sequence and functionally important residues
RT   of 16S rRNA:m(1)A1408 methyltransferase KamB that causes bacterial
RT   resistance to aminoglycoside antibiotics.";
RL   Cell Cycle 6:1268-1271(2007).
CC   -!- FUNCTION: Specifically methylates the N(1) position of adenine 1408 in
CC       16S rRNA. Confers resistance to various aminoglycosides (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1408) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(1)-methyladenosine(1408) in 16S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42776, Rhea:RHEA-COMP:10227, Rhea:RHEA-COMP:10228,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.180;
CC   -!- MISCELLANEOUS: Protects S.hindustanus, which is an antibiotic-producing
CC       bacterium, against self-intoxication.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Kanamycin-
CC       apramycin resistance family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI47641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ875019; CAI47641.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_063964001.1; NZ_FQVN01000008.1.
DR   AlphaFoldDB; Q2MEY3; -.
DR   SMR; Q2MEY3; -.
DR   STRING; 2017.SAMN05444320_108263; -.
DR   BRENDA; 2.1.1.180; 11472.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..215
FT                   /note="16S rRNA (adenine(1408)-N(1))-methyltransferase"
FT                   /id="PRO_0000417016"
FT   BINDING         32
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         87..88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  23670 MW;  AA06B0A625873FC5 CRC64;
     MRRVVGKRVL EFSEAEFDQL RSQYDEVVLD VGTGDGKHPY KVARQHPNQL VVALDADKTR
     MERMSAKAAA KPAKGGLPNL LYLWATAEKL PPLTGVGELH VLMPWGSLLR GILGSSPEML
     RGLAAVCRPD AAFLVALNLH AWRPPVPEVG EHPEPTPETV DEGLAARYAQ AGWQLTDCRY
     LAAEEVAALE TSWTRRLNSS RDRFDVLALT GKINP