ID   PAPA2_MYCBP             Reviewed;         468 AA.
AC   A1KQF4;
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=Trehalose-2-sulfate acyltransferase PapA2 {ECO:0000250|UniProtKB:P9WIK7};
DE            EC=2.3.1.288 {ECO:0000250|UniProtKB:P9WIK7};
DE   AltName: Full=2-O-sulfo trehalose long-chain-acyltransferase {ECO:0000250|UniProtKB:P9WIK7};
DE   AltName: Full=Polyketide synthase-associated protein A2;
GN   Name=papA2; OrderedLocusNames=BCG_3882c;
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 by adding the
CC       palmitoyl group at the 2'-position to yield the intermediate trehalose-
CC       2-sulfate-2'-palmitate (SL659). {ECO:0000250|UniProtKB:P9WIK7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-O-sulfo-alpha,alpha-trehalose + hexadecanoyl-CoA = 2-O-
CC         sulfo-2'-O-hexadecanoyl-alpha,alpha-trehalose + CoA;
CC         Xref=Rhea:RHEA:44060, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:60091, ChEBI:CHEBI:60092; EC=2.3.1.288;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44061;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK7};
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; CAL73872.1; -; Genomic_DNA.
DR   RefSeq; WP_010950943.1; NC_008769.1.
DR   AlphaFoldDB; A1KQF4; -.
DR   SMR; A1KQF4; -.
DR   KEGG; mbb:BCG_3882c; -.
DR   HOGENOM; CLU_034647_0_0_11; -.
DR   OMA; CMWVNRF; -.
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..468
FT                   /note="Trehalose-2-sulfate acyltransferase PapA2"
FT                   /id="PRO_0000314661"
SQ   SEQUENCE   468 AA;  52162 MW;  9163239A64112ED9 CRC64;
     MFSITTLRDW TPDPGSIICW HASPTAKAKA RQAPISEVPP SYQQAQHLRR YRDHVARGLD
     MSRLMIFTWD LPGRCNIRAM NYAINAHLRR HDTYHSWFEF DNAEHIVRHT IADPADIEVV
     QAEHQNMTSA ELRHHIATPQ PLQWDCFLFG IIQSDDHFTF YASIAHLCVD PMIVGVLFIE
     IHMMYSALVG GDPPIELPPA GRYDDHCVRQ YADTAALTLD SARVRRWVEF AANNDGTLPH
     FPLPLGDLSV PHTGKLLTET LMDEQQGERF EAACVAAGAR FSGGVFACAA LAERELTNCE
     TFDVVTTTDT RRTPTELRTT GWFTGLVPIT VPVASGLFDS AARVAQISFD SGKDLATVPF
     DRVLELARPE TGLRPPRPGN FVMSFLDASI APLSTVANSD LNFRIYDEGR VSHQVSMWVN
     RYQHQTTVTV LFPDNPIASE SVANYIAAMK SIYIRTADGT LAILKPGT