ID   PAPA5_MYCUA             Reviewed;         414 AA.
AC   A0PQ31;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Phthiocerol/phthiodiolone dimycocerosyl transferase;
DE            EC=2.3.1.282 {ECO:0000250|UniProtKB:P9WIN5};
DE   AltName: Full=Acyltransferase PapA5;
DE   AltName: Full=Phthiocerol/phthiodiolone O-acyltransferase;
DE   AltName: Full=Polyketide synthase-associated protein A5;
GN   Name=papA5; OrderedLocusNames=MUL_2011;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- FUNCTION: Catalyzes diesterification of phthiocerol, phthiodiolone, and
CC       phenolphthiocerol with mycocerosic acids, the final step in the
CC       phthiocerol, phthiodiolone and phenolphthiocerol dimycocerosate esters
CC       (PDIM) synthesis. Can directly transfer the mycocerosate bound to the
CC       mycocerosic acid synthase (mas) onto the substrate alcohols.
CC       {ECO:0000250|UniProtKB:P9WIN5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a phthiocerol =
CC         a dimycocerosyl phthiocerol + 2 holo-[mycocerosic acid synthase].;
CC         EC=2.3.1.282; Evidence={ECO:0000250|UniProtKB:P9WIN5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a phthiodiolone
CC         = a dimycocerosyl phthiodiolone + 2 holo-[mycocerosic acid
CC         synthase].; EC=2.3.1.282; Evidence={ECO:0000250|UniProtKB:P9WIN5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a mycocerosyl-[mycocerosic acid synthase] + a
CC         phenolphthiocerol = a dimycocerosyl phenolphthiocerol + 2 holo-
CC         [mycocerosic acid synthase].; EC=2.3.1.282;
CC         Evidence={ECO:0000250|UniProtKB:P9WIN5};
CC   -!- SUBUNIT: Monomer. Interacts directly with the acyl carrier protein
CC       (ACP) domain of the mycocerosic acid synthase (mas) protein.
CC       {ECO:0000250|UniProtKB:P9WIN5}.
CC   -!- DOMAIN: Consists of two structural domains that are related to each
CC       other. {ECO:0000250|UniProtKB:P9WIN5}.
CC   -!- SIMILARITY: Belongs to the acyltransferase PapA5 family. {ECO:0000305}.
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DR   EMBL; CP000325; ABL04450.1; -; Genomic_DNA.
DR   RefSeq; WP_011740069.1; NC_008611.1.
DR   AlphaFoldDB; A0PQ31; -.
DR   SMR; A0PQ31; -.
DR   STRING; 362242.MUL_2011; -.
DR   EnsemblBacteria; ABL04450; ABL04450; MUL_2011.
DR   KEGG; mul:MUL_2011; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_050374_1_0_11; -.
DR   OMA; EMFAETH; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR031641; PapA_C.
DR   Pfam; PF16911; PapA_C; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipid biosynthesis; Lipid metabolism; Transferase.
FT   CHAIN           1..414
FT                   /note="Phthiocerol/phthiodiolone dimycocerosyl transferase"
FT                   /id="PRO_0000332109"
FT   ACT_SITE        118
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   SITE            122
FT                   /note="Structural role in the organization of the active
FT                   site"
FT                   /evidence="ECO:0000250"
FT   SITE            304
FT                   /note="Important for mas ACP domain recognition"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   414 AA;  45394 MW;  AC671512AB35C6A4 CRC64;
     MFPGAVIRKL AFSEEIYARY QAFTSFTAHV RGPVDIDAMS EAFDALLQAH PVFAAHLEEG
     PDGNHHIVAN DLLHSGLVVI DGRRAENPHV QLDQRDSLFR LQLTLGESEN LVTAYVHHSL
     ADAHHLGSLL DELLSRYTDV VTTGDPGPIT PEPAPQPAED LLKRRGIKQS ALTGFERFLP
     LLFAYDLPPI AEEMRKFEAP EPVPVTRCRL TSQETADLVS FSRDNGLSFN AVLAAAILLA
     EWRLRETPHV PIPYCYAVDL RFLLSPPVGA TESTNPVGLA TYLAEIGPDT DITELAADIV
     ATFRADLSDG MIHQSALRSG RILEGTPPGL PPFILCTNVS TLPPIRTPED VELVDFHSRI
     HCAMDVPFGF YACSIATDRL SIELHGSIPA PQLLLDAIRD ILCSVPSEYG LFME