KAMB_STRSD
ID KAMB_STRSD Reviewed; 215 AA.
AC P25920; Q2MFK4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=16S rRNA (adenine(1408)-N(1))-methyltransferase;
DE EC=2.1.1.180;
DE AltName: Full=16S rRNA m1A1408 methyltransferase;
DE AltName: Full=Kanamycin-apramycin resistance methylase;
GN Name=kamB;
OS Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 /
OS CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1)
OS (Streptomyces tenebrarius).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Streptoalloteichus.
OX NCBI_TaxID=1933;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16175 / NCIMB
RC 11028 / NRRL B-12390 / A12253. 1;
RX PubMed=1840536; DOI=10.1016/0378-1119(91)90532-g;
RA Holmes D.J., Drocourt D., Tiraby G., Cundiffe E.;
RT "Cloning of an aminoglycoside-resistance-encoding gene, kamC, from
RT Saccharopolyspora hirsuta: comparison with kamB from Streptomyces
RT tenebrarius.";
RL Gene 102:19-26(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16175 / NCIMB
RC 11028 / NRRL B-12390 / A12253. 1;
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 (Streptomyces tenebrarius DSM 40477)
RT and hygromycin B (Streptomyces hygroscopicus subsp. hygroscopicus DSM
RT 40578), which contain genes related to both the biosynthesis of other
RT aminoglycosides and cell-wall sugars.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN ANTIBIOTIC RESISTANCE, AND IDENTIFICATION OF START SITE.
RX PubMed=19589804; DOI=10.1093/nar/gkp575;
RA Savic M., Lovric J., Tomic T.I., Vasiljevic B., Conn G.L.;
RT "Determination of the target nucleosides for members of two families of 16S
RT rRNA methyltransferases that confer resistance to partially overlapping
RT groups of aminoglycoside antibiotics.";
RL Nucleic Acids Res. 37:5420-5431(2009).
RN [4]
RP FUNCTION, AND CRYSTALLIZATION.
RX PubMed=20667473; DOI=10.1016/j.pep.2010.07.005;
RA Zelinskaya N., Rankin C.R., Macmaster R., Savic M., Conn G.L.;
RT "Expression, purification and crystallization of adenosine 1408
RT aminoglycoside-resistance rRNA methyltransferases for structural studies.";
RL Protein Expr. Purif. 75:89-94(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, AND MUTAGENESIS OF ARG-8; ASP-30;
RP LYS-37; ASP-55; LYS-58; ARG-60; LYS-63; LYS-67; LYS-71; LYS-74; GLU-88;
RP TRP-105; SER-107; ASN-138; LYS-174; ARG-179; THR-191; TRP-193; ARG-195;
RP ARG-196; ARG-201 AND ARG-203.
RC STRAIN=ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16175 / NCIMB
RC 11028 / NRRL B-12390 / A12253. 1;
RX PubMed=20639535; DOI=10.1093/nar/gkq627;
RA Macmaster R., Zelinskaya N., Savic M., Rankin C.R., Conn G.L.;
RT "Structural insights into the function of aminoglycoside-resistance A1408
RT 16S rRNA methyltransferases from antibiotic-producing and human pathogenic
RT bacteria.";
RL Nucleic Acids Res. 38:7791-7799(2010).
CC -!- FUNCTION: Specifically methylates the N(1) position of adenine 1408 in
CC 16S rRNA. Confers resistance to various aminoglycosides, including
CC kanamycin, neomycin and apramycin. {ECO:0000269|PubMed:19589804,
CC ECO:0000269|PubMed:20639535, ECO:0000269|PubMed:20667473}.
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 Streptomyces, 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=AAA26774.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAF33037.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M64625; AAA26774.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ629123; CAF33037.1; ALT_INIT; Genomic_DNA.
DR PIR; JQ1137; JQ1137.
DR RefSeq; WP_063964000.1; NG_050561.1.
DR PDB; 3MQ2; X-ray; 1.69 A; A/B=1-215.
DR PDBsum; 3MQ2; -.
DR AlphaFoldDB; P25920; -.
DR SMR; P25920; -.
DR BRENDA; 2.1.1.180; 7970.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..215
FT /note="16S rRNA (adenine(1408)-N(1))-methyltransferase"
FT /id="PRO_0000068566"
FT BINDING 32
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:20639535"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:20639535"
FT BINDING 87..88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:20639535"
FT BINDING 102..107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:20639535"
FT BINDING 191..193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:20639535"
FT MUTAGEN 8
FT /note="R->A: No change in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 30
FT /note="D->A: Loss of kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 37
FT /note="K->A: Loss of kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 55
FT /note="D->A: Loss of kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 58
FT /note="K->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 60
FT /note="R->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 63
FT /note="K->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 67
FT /note="K->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 71
FT /note="K->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 74
FT /note="K->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 88
FT /note="E->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 105
FT /note="W->A,F: Loss of kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 107
FT /note="S->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 138
FT /note="N->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 174
FT /note="K->A: No change in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 179
FT /note="R->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 191
FT /note="T->A: Loss of kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 193
FT /note="W->A,F: Loss of kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 195
FT /note="R->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 196
FT /note="R->A: Loss of kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 201
FT /note="R->A: Loss of kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT MUTAGEN 203
FT /note="R->A: Decrease in kanamycin resistance."
FT /evidence="ECO:0000269|PubMed:20639535"
FT CONFLICT 75..76
FT /note="GG -> A (in Ref. 1; AAA26774)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..145
FT /note="ALNLHAWRPS -> ECNRSCRGPP (in Ref. 1; AAA26774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 215 AA; 23664 MW; 8B721057CAF6F377 CRC64;
MRRVVGKRVQ EFSDAEFEQL RSQYDDVVLD VGTGDGKHPY KVARQNPSRL VVALDADKSR
MEKISAKAAA KPAKGGLPNL LYLWATAERL PPLSGVGELH VLMPWGSLLR GVLGSSPEML
RGMAAVCRPG ASFLVALNLH AWRPSVPEVG EHPEPTPDSA DEWLAPRYAE AGWKLADCRY
LEPEEVAGLE TSWTRRLHSS RDRFDVLALT GTISP
