ID   PAPA1_MYCTA             Reviewed;         511 AA.
AC   A5U9F3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
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};
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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 H37Ra, 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; CP000611; ABQ75653.1; -; Genomic_DNA.
DR   RefSeq; WP_003899711.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U9F3; -.
DR   SMR; A5U9F3; -.
DR   STRING; 419947.MRA_3864; -.
DR   EnsemblBacteria; ABQ75653; ABQ75653; MRA_3864.
DR   KEGG; mra:MRA_3864; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_034647_1_0_11; -.
DR   OMA; AEIHLMY; -.
DR   OrthoDB; 1163259at2; -.
DR   Proteomes; UP000001988; 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_0000314659"
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