ID   OLSG_SINAD              Reviewed;         192 AA.
AC   L0D9B6;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Ornithine lipid N-methyltransferase {ECO:0000303|PubMed:25925947};
DE            Short=OL N-methyltransferase {ECO:0000303|PubMed:25925947};
DE            EC=2.1.1.344 {ECO:0000269|PubMed:25925947};
DE   AltName: Full=Ornithine lipid synthesis G {ECO:0000303|PubMed:25925947};
GN   Name=olsG {ECO:0000303|PubMed:25925947};
GN   OrderedLocusNames=Sinac_1600 {ECO:0000312|EMBL:AGA25979.1};
OS   Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS   MOB10).
OC   Bacteria; Planctomycetes; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Singulisphaera.
OX   NCBI_TaxID=886293;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10;
RX   PubMed=25925947; DOI=10.1074/jbc.m115.639575;
RA   Escobedo-Hinojosa W.I., Vences-Guzman M.A., Schubotz F.,
RA   Sandoval-Calderon M., Summons R.E., Lopez-Lara I.M., Geiger O.,
RA   Sohlenkamp C.;
RT   "OlsG (Sinac_1600) is an ornithine lipid N-methyltransferase from the
RT   planctomycete Singulisphaera acidiphila.";
RL   J. Biol. Chem. 290:15102-15111(2015).
CC   -!- FUNCTION: Catalyzes the 3-fold methylation of ornithine lipids. Forms
CC       ornithine lipids that are mono-, di-, and trimethylated on the delta-
CC       nitrogen of the ornithine head group. {ECO:0000269|PubMed:25925947}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(2)-[(3R)-3-(2-saturated-acyloxy)acyl]-L-ornithine lipid +
CC         3 S-adenosyl-L-methionine = an N,N,N-trimethylornithine lipid + 3
CC         H(+) + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:20461,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138473, ChEBI:CHEBI:138481; EC=2.1.1.344;
CC         Evidence={ECO:0000269|PubMed:25925947};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20462;
CC         Evidence={ECO:0000269|PubMed:25925947};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:25925947};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP003364; AGA25979.1; -; Genomic_DNA.
DR   RefSeq; WP_015245149.1; NZ_JH621477.1.
DR   AlphaFoldDB; L0D9B6; -.
DR   SMR; L0D9B6; -.
DR   STRING; 886293.Sinac_1600; -.
DR   EnsemblBacteria; AGA25979; AGA25979; Sinac_1600.
DR   KEGG; saci:Sinac_1600; -.
DR   eggNOG; COG3963; Bacteria.
DR   HOGENOM; CLU_085338_2_1_0; -.
DR   OMA; RIWMNLP; -.
DR   OrthoDB; 2030110at2; -.
DR   BioCyc; MetaCyc:MON-20224; -.
DR   BRENDA; 2.1.1.344; 15331.
DR   Proteomes; UP000010798; Chromosome.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; PTHR11727; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..192
FT                   /note="Ornithine lipid N-methyltransferase"
FT                   /id="PRO_0000447009"
SQ   SEQUENCE   192 AA;  22068 MW;  D6335D31FC00EB67 CRC64;
     MKDFFLFLGK FFKHGTAIAS LAPSSPWLSR TTVRNIPWEN ARVVVELGAG TGPITKVIAD
     RVHPDCRVIV LERDPDFARL LRERFANRAN FDVVEGDVRD LTQILQQRGI EQADFVVSGL
     PVPSFPKELQ RDLFRVVKQV LAPSGTFNQI TEMPWVYQRF YRRFFDEVTF VFEPRNLPPA
     GAYFCRGVKE SF