ID   PAPA1_MYCBP             Reviewed;         511 AA.
AC   A1KQF9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=2'-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase PapA1 {ECO:0000250|UniProtKB:P9WIK9};
DE            EC=2.3.1.283 {ECO:0000250|UniProtKB:P9WIK9};
DE   AltName: Full=Polyketide synthase-associated protein A1;
DE   AltName: Full=SL659 acyltransferase PapA1 {ECO:0000250|UniProtKB:P9WIK9};
GN   Name=papA1; OrderedLocusNames=BCG_3887c;
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 the acylation of trehalose-2-sulfate-2'-palmitate
CC       (SL659) by adding the (hydroxy)phthioceranoyl group at the 3'-position
CC       to yield the diacylated intermediate 2-palmitoyl-3-(C43)-phthioceranyl-
CC       alpha, alpha'-D-trehalose-2'-sulfate (SL1278).
CC       {ECO:0000250|UniProtKB:P9WIK9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid
CC         synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose = a
CC         3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-
CC         alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase].;
CC         EC=2.3.1.283; Evidence={ECO:0000250|UniProtKB:P9WIK9};
CC   -!- MISCELLANEOUS: In strain BCG, the sulfolipid-1 (SL-1) is not
CC       synthesized.
CC   -!- SIMILARITY: Belongs to the PapA acyltransferase family. {ECO:0000305}.
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DR   EMBL; AM408590; CAL73877.1; -; Genomic_DNA.
DR   RefSeq; WP_003899711.1; NC_008769.1.
DR   AlphaFoldDB; A1KQF9; -.
DR   SMR; A1KQF9; -.
DR   KEGG; mbb:BCG_3887c; -.
DR   HOGENOM; CLU_034647_1_0_11; -.
DR   OMA; AEIHLMY; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   Pfam; PF00668; Condensation; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..511
FT                   /note="2'-acyl-2-O-sulfo-trehalose
FT                   (hydroxy)phthioceranyltransferase PapA1"
FT                   /id="PRO_0000314657"
SQ   SEQUENCE   511 AA;  56128 MW;  07D7766EF181C4E5 CRC64;
     MRIGPVELSA VKDWDPAPGV LVSWHPTPAS CAKALAAPVS AVPPSYVQAR QIRSFSEQAA
     RGLDHSRLLI ASVEVFGHCD LRAMTYVINA HLRRHDTYRS WFELRDTDHI VRHSIADPAD
     IEFVPTTHGE MTSADLRQHI VATPDSLHWD CFSFGVIQRA DSFTFYASID HLHADGQFVG
     VGLMEFQSMY TALIMGEPPI GLSEAGSYVD FCVRQHEYTS ALTVDSPEVR AWIDFAEINN
     GTFPEFPLPL GDPSVRCGGD LLSMMLMDEQ QTQRFESACM AANARFIGGM LACIAIAIHE
     LTGADTYFGI TPKDIRTPAD LMTQGWFTGQ IPVTVPVAGL SFNEIARIAQ TSFDTGADLA
     KVPFERVVEL SPSLRRPQPL FSLVNFFDAQ VGPLSAVTKL FEGLNVGTYS DGRVTYPLST
     MVGRFDETAA SVLFPDNPVA RESVTAYLRA IRSVCMRIAN GGTAERVGNV VALSPGRRNN
     IERMTWRSCR AGDFIDICNL KVANVTVDRE A