ID   OCTT_MYCTU              Reviewed;         247 AA.
AC   P71725; F2GI29; I6Y0P0; Q7D765;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Diglucosylglycerate octanoyltransferase {ECO:0000303|PubMed:26324178};
DE            Short=DGG octanoyltransferase {ECO:0000303|PubMed:26324178};
DE            EC=2.3.1.273 {ECO:0000250|UniProtKB:K5BJH8};
GN   Name=octT {ECO:0000303|PubMed:26324178};
GN   OrderedLocusNames=Rv2418c {ECO:0000312|EMBL:CCP45209.1};
GN   ORFNames=LH57_13210 {ECO:0000312|EMBL:AIR15182.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA   Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA   Monaco A., King S., Sohrabi A.;
RT   "Phylogenetic analysis of Mycobacterial species using whole genome
RT   sequences.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
RN   [4]
RP   FUNCTION, AND SUBUNIT.
RC   STRAIN=H37Rv;
RX   PubMed=26324178; DOI=10.1038/srep13610;
RA   Maranha A., Moynihan P.J., Miranda V., Correia Lourenco E., Nunes-Costa D.,
RA   Fraga J.S., Jose Barbosa Pereira P., Macedo-Ribeiro S., Ventura M.R.,
RA   Clarke A.J., Empadinhas N.;
RT   "Octanoylation of early intermediates of mycobacterial methylglucose
RT   lipopolysaccharides.";
RL   Sci. Rep. 5:13610-13610(2015).
CC   -!- FUNCTION: Sugar octanoyltransferase likely involved in the biosynthesis
CC       of mycobacterial methylglucose lipopolysaccharide (MGLP). Catalyzes the
CC       transfer of an octanoyl group from octanoyl-CoA to the C6 OH of the
CC       second glucose in diglucosylglycerate (DGG). DGG is the preferred
CC       acceptor, but to a lesser extent, GG (glucosylglycerate) can also be
CC       used as substrate. DGG and GG are the two earliest intermediates in
CC       MGLP biosynthesis. {ECO:0000250|UniProtKB:K5BJH8,
CC       ECO:0000305|PubMed:26324178}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-
CC         glucopyranosyl]-glycerate + octanoyl-CoA = (2R)-2-O-[6-O-octanoyl-
CC         alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-glycerate +
CC         CoA; Xref=Rhea:RHEA:56868, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC         ChEBI:CHEBI:141056, ChEBI:CHEBI:141058; EC=2.3.1.273;
CC         Evidence={ECO:0000250|UniProtKB:K5BJH8};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:26324178}.
CC   -!- SIMILARITY: Belongs to the OctT acyltransferase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP45209.1; -; Genomic_DNA.
DR   EMBL; CP009480; AIR15182.1; -; Genomic_DNA.
DR   RefSeq; NP_216934.1; NC_000962.3.
DR   RefSeq; WP_003412384.1; NZ_NVQJ01000054.1.
DR   AlphaFoldDB; P71725; -.
DR   STRING; 83332.Rv2418c; -.
DR   PaxDb; P71725; -.
DR   PRIDE; P71725; -.
DR   GeneID; 45426405; -.
DR   GeneID; 885304; -.
DR   KEGG; mtu:Rv2418c; -.
DR   PATRIC; fig|83332.111.peg.2703; -.
DR   TubercuList; Rv2418c; -.
DR   eggNOG; COG2755; Bacteria.
DR   HOGENOM; CLU_1106189_0_0_11; -.
DR   OMA; IMSGRGN; -.
DR   BRENDA; 2.3.1.273; 3445.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0016414; F:O-octanoyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR036514; SGNH_hydro_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..247
FT                   /note="Diglucosylglycerate octanoyltransferase"
FT                   /id="PRO_0000436913"
SQ   SEQUENCE   247 AA;  27225 MW;  B450E792E291F124 CRC64;
     MSSRRGRRPA LLVFADSLAY YGPTGGLPAD DPRIWPNIVA SQLDWDLELI GRIGWTCRDV
     WWAATQDPRA WAALPRAGAV IFATGGMDSL PSVLPTALRE LIRYVRPSWL RRWVRDGYAW
     VQPRLSPVAR AALPPHLTAE YLEKTRGAID FNRPGIPIIA SLPSVHIAET YGKAHHGRAG
     TVAAITEWAQ HHDIPLVDLK AAVAEQILSG YGNRDGIHWN FEAHQAVAEL MLKALAEAGV
     PNEKSRG