ID   PAPA5_MYCBP             Reviewed;         422 AA.
AC   A1KMT4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=BCG_2961;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(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}.
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; AM408590; CAL72950.1; -; Genomic_DNA.
DR   RefSeq; WP_003414853.1; NC_008769.1.
DR   AlphaFoldDB; A1KMT4; -.
DR   SMR; A1KMT4; -.
DR   GeneID; 45426927; -.
DR   KEGG; mbb:BCG_2961; -.
DR   HOGENOM; CLU_050374_1_0_11; -.
DR   OMA; EMFAETH; -.
DR   Proteomes; UP000001472; 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..422
FT                   /note="Phthiocerol/phthiodiolone dimycocerosyl transferase"
FT                   /id="PRO_0000332103"
FT   ACT_SITE        124
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   SITE            128
FT                   /note="Structural role in the organization of the active
FT                   site"
FT                   /evidence="ECO:0000250"
FT   SITE            312
FT                   /note="Important for mas ACP domain recognition"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  45429 MW;  19156C6B9FCC3AA7 CRC64;
     MFPGSVIRKL SHSEEVFAQY EVFTSMTIQL RGVIDVDALS DAFDALLETH PVLASHLEQS
     SDGGWNLVAD DLLHSGICVI DGTAATNGSP SGNAELRLDQ SVSLLHLQLI LREGGAELTL
     YLHHCMADGH HGAVLVDELF SRYTDAVTTG DPGPITPQPT PLSMEAVLAQ RGIRKQGLSG
     AERFMSVMYA YEIPATETPA VLAHPGLPQA VPVTRLWLSK QQTSDLMAFG REHRLSLNAV
     VAAAILLTEW QLRNTPHVPI PYVYPVDLRF VLAPPVAPTE ATNLLGAASY LAEIGPNTDI
     VDLASDIVAT LRADLANGVI QQSGLHFGTA FEGTPPGLPP LVFCTDATSF PTMRTPPGLE
     IEDIKGQFYC SISVPLDLYS CAVYAGQLII EHHGHIAEPG KSLEAIRSLL CTVPSEYGWI
     ME