ID   Y1506_MYCTU             Reviewed;         166 AA.
AC   P71785; F2GEJ7; I6XBN0; L0T9U1;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Putative methyltransferase Rv1506c {ECO:0000303|PubMed:20844580};
DE            EC=2.1.1.- {ECO:0000303|PubMed:20844580};
GN   OrderedLocusNames=Rv1506c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Beijing GC1237;
RX   PubMed=20844580; DOI=10.1371/journal.ppat.1001100;
RA   Brodin P., Poquet Y., Levillain F., Peguillet I., Larrouy-Maumus G.,
RA   Gilleron M., Ewann F., Christophe T., Fenistein D., Jang J., Jang M.S.,
RA   Park S.J., Rauzier J., Carralot J.P., Shrimpton R., Genovesio A.,
RA   Gonzalo-Asensio J.A., Puzo G., Martin C., Brosch R., Stewart G.R.,
RA   Gicquel B., Neyrolles O.;
RT   "High content phenotypic cell-based visual screen identifies Mycobacterium
RT   tuberculosis acyltrehalose-containing glycolipids involved in phagosome
RT   remodeling.";
RL   PLoS Pathog. 6:E1001100-E1001100(2010).
CC   -!- FUNCTION: Probably plays a role in host phagosome maturation arrest, as
CC       well as a role in the synthesis of acyltrehalose-containing glycolipids
CC       (PubMed:20844580). {ECO:0000305|PubMed:20844580}.
CC   -!- DISRUPTION PHENOTYPE: Grows normally in liquid culture, traffics into
CC       host (human and mouse) acidified compartments early after phagocytosis,
CC       suggesting it no longer arrests phagosome maturation as well as wild-
CC       type, impaired growth in mouse macrophages (PubMed:20844580). Decreased
CC       synthesis of 2,3-di-O-acyltrehaloses (DAT) and increased synthesis of
CC       sulfoglycolipids (SGL) (PubMed:20844580). Decreased colonization of
CC       mouse lung but not spleen 42 days after infection (PubMed:20844580).
CC       {ECO:0000269|PubMed:20844580}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {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; AL123456; CCP44268.1; -; Genomic_DNA.
DR   RefSeq; NP_216022.1; NC_000962.3.
DR   RefSeq; WP_003902091.1; NC_000962.3.
DR   AlphaFoldDB; P71785; -.
DR   SMR; P71785; -.
DR   STRING; 83332.Rv1506c; -.
DR   PaxDb; P71785; -.
DR   PRIDE; P71785; -.
DR   DNASU; 886479; -.
DR   GeneID; 886479; -.
DR   KEGG; mtu:Rv1506c; -.
DR   PATRIC; fig|83332.111.peg.1678; -.
DR   TubercuList; Rv1506c; -.
DR   eggNOG; COG4106; Bacteria.
DR   OMA; IGIDIMP; -.
DR   PhylomeDB; P71785; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IDA:MTBBASE.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0052170; P:suppression by symbiont of host innate immune response; IDA:MTBBASE.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..166
FT                   /note="Putative methyltransferase Rv1506c"
FT                   /id="PRO_0000438346"
SQ   SEQUENCE   166 AA;  18580 MW;  BB2BD75F91F6EB52 CRC64;
     MRIVNAADPF SINDLGCGYG ALLDYLDARG FKTDYTGIDV SPEMVRAAAL RFEGRANADF
     ICAARIDREA DYSVASGIFN VRLKSLDTEW CAHIEATLDM LNAASRRGFS FNCLTSYSDA
     SKMRDDLYYA DPCALFDLCK RRYSKSVALL HDYGLYEFTI LVRKAS