ID   Y3087_MYCTU             Reviewed;         472 AA.
AC   P9WKB1; L0TBI7; O53304;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Putative diacyglycerol O-acyltransferase Rv3087;
DE            EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE   AltName: Full=Putative triacylglycerol synthase Rv3087;
GN   OrderedLocusNames=Rv3087; ORFNames=MTV013.08;
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   INDUCTION.
RX   PubMed=14568148; DOI=10.1016/s0378-1097(03)00648-7;
RA   Singh A., Jain S., Gupta S., Das T., Tyagi A.K.;
RT   "mymA operon of Mycobacterium tuberculosis: its regulation and importance
RT   in the cell envelope.";
RL   FEMS Microbiol. Lett. 227:53-63(2003).
RN   [3]
RP   FUNCTION IN E.COLI, CATALYTIC ACTIVITY, AND INDUCTION BY NITRIC OXIDE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15262939; DOI=10.1128/jb.186.15.5017-5030.2004;
RA   Daniel J., Deb C., Dubey V.S., Sirakova T.D., Abomoelak B., Morbidoni H.R.,
RA   Kolattukudy P.E.;
RT   "Induction of a novel class of diacylglycerol acyltransferases and
RT   triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into
RT   a dormancy-like state in culture.";
RL   J. Bacteriol. 186:5017-5030(2004).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Erdman;
RX   PubMed=15937179; DOI=10.1128/jb.187.12.4173-4186.2005;
RA   Singh A., Gupta R., Vishwakarma R.A., Narayanan P.R., Paramasivan C.N.,
RA   Ramanathan V.D., Tyagi A.K.;
RT   "Requirement of the mymA operon for appropriate cell wall ultrastructure
RT   and persistence of Mycobacterium tuberculosis in the spleens of guinea
RT   pigs.";
RL   J. Bacteriol. 187:4173-4186(2005).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=16893682; DOI=10.1016/j.tube.2006.01.021;
RA   Cheruvu M., Plikaytis B.B., Shinnick T.M.;
RT   "The acid-induced operon Rv3083-Rv3089 is required for growth of
RT   Mycobacterium tuberculosis in macrophages.";
RL   Tuberculosis 87:12-20(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Required for maintaining the appropriate mycolic acid
CC       composition and permeability of the envelope on its exposure to acidic
CC       pH. Upon expression in E.coli functions weakly as a triacylglycerol
CC       synthase, making triacylglycerol (TG) from diolein and long-chain fatty
CC       acyl-CoA. Has no wax synthase activity. {ECO:0000269|PubMed:15262939,
CC       ECO:0000269|PubMed:15937179}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC         + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC         Evidence={ECO:0000269|PubMed:15262939};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + di-(9Z)-octadecenoylglycerol = 1,2,3-
CC         tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:45780,
CC         ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:15262939};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45781;
CC         Evidence={ECO:0000269|PubMed:15262939};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- INDUCTION: Expression is controlled by VirS. Induced at acidic pH and
CC       in macrophages, and in response to low levels of nitric oxide (NO).
CC       {ECO:0000269|PubMed:14568148, ECO:0000269|PubMed:15262939}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of the mymA operon causes altered
CC       cell wall structure, reduced contents and altered composition of
CC       mycolic acids along with the accumulation of saturated C24 and C26
CC       fatty acids, and enhanced susceptibility to antibiotics, detergents and
CC       acidic pH. Also impairs ability to survive in macrophages.
CC       {ECO:0000269|PubMed:15937179, ECO:0000269|PubMed:16893682}.
CC   -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45896.1; -; Genomic_DNA.
DR   PIR; C70853; C70853.
DR   RefSeq; NP_217603.1; NC_000962.3.
DR   RefSeq; WP_003906978.1; NZ_NVQJ01000011.1.
DR   AlphaFoldDB; P9WKB1; -.
DR   SMR; P9WKB1; -.
DR   STRING; 83332.Rv3087; -.
DR   SwissLipids; SLP:000001176; -.
DR   PaxDb; P9WKB1; -.
DR   DNASU; 888653; -.
DR   GeneID; 888653; -.
DR   KEGG; mtu:Rv3087; -.
DR   TubercuList; Rv3087; -.
DR   eggNOG; COG1020; Bacteria.
DR   OMA; WEFHFAE; -.
DR   PhylomeDB; P9WKB1; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010447; P:response to acidic pH; IEP:MTBBASE.
DR   GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR   GO; GO:0071731; P:response to nitric oxide; IBA:GO_Central.
DR   GO; GO:0052562; P:suppression by symbiont of host immune response; IDA:MTBBASE.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR014292; Acyl_transf_WS/DGAT.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR   InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR   InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR   PANTHER; PTHR31650; PTHR31650; 1.
DR   Pfam; PF03007; WES_acyltransf; 1.
DR   Pfam; PF06974; WS_DGAT_C; 1.
DR   TIGRFAMs; TIGR02946; acyl_WS_DGAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Glycerol metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..472
FT                   /note="Putative diacyglycerol O-acyltransferase Rv3087"
FT                   /id="PRO_0000222913"
FT   REGION          217..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   472 AA;  52597 MW;  AC03BDDB4970FCC0 CRC64;
     MRRLNGVDAL MLYLDGGSAY NHTLKISVLD PSTDPDGWSW PKARQMFEER AHLLPVFRLR
     YLPTPLGLHH PIWVEDPEFD LDAHVRRVVC PAPGGMAEFC ALVEQIYAHP LDRDRPLWQT
     WVVEGLDGGR VALVTLLHHA YSDGVGVLDM LAAFYNDTPD EAPVVAPPWE PPPLPSTRQR
     LGWALRDLPS RLGKIAPTVR AVRDRVRIER EFAKDGDRRV PPTFDRSAPP GPFQRGLSRS
     RRFSCESFPL AEVREVSKTL GVTINDVFLA CVAGAVRRYL ERCGSPPTDA MVATMPLAVT
     PAAERAHPGN YSSVDYVWLR ADIADPLERL HATHLAAEAT KQHFAQTKDA DVGAVVELLP
     ERLISGLARA NARTKGRFDT FKNVVVSNVP GPREPRYLGR WRVDQWFSTG QISHGATLNM
     TVWSYCDQFN LCVMADAVAV RNTWELLGGF RASHEELLAA ARAQATPKEM AT