ID   PAPA5_MYCSK             Reviewed;         410 AA.
AC   A1UGV8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Mkms_2872;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL92066.1; -; Genomic_DNA.
DR   RefSeq; WP_011768239.1; NC_008705.1.
DR   AlphaFoldDB; A1UGV8; -.
DR   SMR; A1UGV8; -.
DR   STRING; 189918.Mkms_2872; -.
DR   EnsemblBacteria; ABL92066; ABL92066; Mkms_2872.
DR   KEGG; mkm:Mkms_2872; -.
DR   HOGENOM; CLU_050374_1_0_11; -.
DR   OMA; EMFAETH; -.
DR   OrthoDB; 1068442at2; -.
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..410
FT                   /note="Phthiocerol/phthiodiolone dimycocerosyl transferase"
FT                   /id="PRO_0000332106"
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"
SQ   SEQUENCE   410 AA;  44501 MW;  01227766E4F2559A CRC64;
     MAYSTSVIRR LAPSEKFFAE TQTFTSITVL LDGTVDIDAM ADAFDALLEA YPVYAGHLEP
     DSDGGFELVA DDLLHPGLWV QFEGDPAPTD QLDQGVALIY LLVKPDSTPV EVTLFIHHSL
     ADGTHMAGLL FELFARYTEV VTTGSAGPVS PNPAPEPIET VLEQRGIRKQ QRSGLDRFIP
     AMFAYELPPK RVTTRSAAER PAAVPTTRCR LSKAETSSLV KYGRVNRLFV NNLISAAILL
     AEWQVRRTPH IPIPYVYNVN LRALVEPPVS ATGCTLAIGV ATYLAHITPQ TTMVELARGI
     ADMFQADLAD GVVQQSLLHF NMQYEGAIPG LPDVVLSTNL GNAVAMSTPP GLEVVGVQSQ
     FYRASSAVID VYSFGVVGGE LLIEHHVDAA ETTIDLIRSL LRSVVSEHQH