ID   PAPA1_MYCTO             Reviewed;         511 AA.
AC   P9WIK8; L0TDN6; O07799; Q7D4T1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
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=MT3932;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Required for the biosynthesis of sulfolipid-1 (SL-1), a major
CC       mycobacterial cell wall lipid. Catalyzes the acylation of trehalose-2-
CC       sulfate-2'-palmitate (SL659) by adding the (hydroxy)phthioceranoyl
CC       group at the 3'-position to yield the diacylated intermediate 2-
CC       palmitoyl-3-(C43)-phthioceranyl-alpha, alpha'-D-trehalose-2'-sulfate
CC       (SL1278). {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   -!- SIMILARITY: Belongs to the PapA acyltransferase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48299.1; -; Genomic_DNA.
DR   PIR; D70522; D70522.
DR   RefSeq; WP_010924723.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIK8; -.
DR   SMR; P9WIK8; -.
DR   EnsemblBacteria; AAK48299; AAK48299; MT3932.
DR   KEGG; mtc:MT3932; -.
DR   PATRIC; fig|83331.31.peg.4230; -.
DR   HOGENOM; CLU_034647_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; 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; Cell wall biogenesis/degradation; Lipid biosynthesis;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..511
FT                   /note="2'-acyl-2-O-sulfo-trehalose
FT                   (hydroxy)phthioceranyltransferase PapA1"
FT                   /id="PRO_0000427989"
SQ   SEQUENCE   511 AA;  56110 MW;  552F19E809EF4649 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 AANARFIGGI LACIAIAIHE
     LTGADTYFGI TPKDIRTPAD LMTQGWFTGQ IPVTVPVAGL SFNEIARIAQ TSFDTGADLA
     KVPFERVVEL SPSLRRPQPL FSLVNFFDAQ VGPLSAVTKL FEGLNVGTYS DGRVTYPLST
     MVGRFDETAA SVLFPDNPVA RESVTAYLRA IRSVCMRIAN GGTAERVGNV VALSPGRRNN
     IERMTWRSCR AGDFIDICNL KVANVTVDRE A