TGS4_MYCTU
ID TGS4_MYCTU Reviewed; 474 AA.
AC P9WKC3; L0TBT5; O53305; P67208;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Probable diacyglycerol O-acyltransferase Tgs4;
DE Short=TGS4;
DE EC=2.3.1.20 {ECO:0000269|PubMed:15262939};
DE AltName: Full=Probable triacylglycerol synthase tgs4;
GN Name=tgs4; OrderedLocusNames=Rv3088; ORFNames=MTV013.09;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 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 as a triacylglycerol synthase,
CC making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA.
CC Has very weak wax synthase activity, incorporating palmityl alcohol
CC into wax esters in the presence of palmitoyl-CoA.
CC {ECO:0000269|PubMed:15262939, 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.2. {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. Induced by low levels of nitric oxide (NO), but not by
CC hypoxia. {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; CCP45897.1; -; Genomic_DNA.
DR PIR; D70853; D70853.
DR RefSeq; NP_217604.1; NC_000962.3.
DR RefSeq; WP_003416079.1; NZ_NVQJ01000011.1.
DR AlphaFoldDB; P9WKC3; -.
DR SMR; P9WKC3; -.
DR STRING; 83332.Rv3088; -.
DR SwissLipids; SLP:000001149; -.
DR PaxDb; P9WKC3; -.
DR DNASU; 888669; -.
DR GeneID; 888669; -.
DR KEGG; mtu:Rv3088; -.
DR TubercuList; Rv3088; -.
DR eggNOG; COG1020; Bacteria.
DR OMA; GHPLWEC; -.
DR PhylomeDB; P9WKC3; -.
DR BRENDA; 2.3.1.20; 3445.
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; IDA:MTBBASE.
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:0045017; P:glycerolipid biosynthetic process; IDA:MTBBASE.
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; IEP:MTBBASE.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:MTBBASE.
DR InterPro; IPR014292; Acyl_transf_WS/DGAT.
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..474
FT /note="Probable diacyglycerol O-acyltransferase Tgs4"
FT /id="PRO_0000222914"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 474 AA; 50887 MW; 36832D972BE3851A CRC64;
MTRINPIDLS FLLLERANRP NHMAAYTIFE KPKGQKSSFG PRLFDAYRHS QAAKPFNHKL
KWLGTDVAAW ETVEPDMGYH IRHLALPAPG SMQQFHETVS FLNTGLLDRG HPMWECYIID
GIERGRIAIL LKVHHALIDG EGGLRAMRNF LSDSPDDTTL AGPWMSAQGA DRPRRTPATV
SRRAQLQGQL QGMIKGLTKL PSGLFGVSAD AADLGAQALS LKARKASLPF TARRTLFNNT
AKSAARAYGN VELPLADVKA LAKATGTSVN DVVMTVIDDA LHHYLAEHQA STDRPLVAFM
PMSLREKSGE GGGNRVSAEL VPMGAPKASP VERLKEINAA TTRAKDKGRG MQTTSRQAYA
LLLLGSLTVA DALPLLGKLP SANVVISNMK GPTEQLYLAG APLVAFSGLP IVPPGAGLNV
TFASINTALC IAIGAAPEAV HEPSRLAELM QRAFTELQTE AGTTSPTTSK SRTP
