ID   PAPA2_MYCTO             Reviewed;         468 AA.
AC   P9WIK6; L0TDW1; Q79F94; Q7D4T4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
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=MT3928;
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 by adding the palmitoyl group at the 2'-position to yield the
CC       intermediate trehalose-2-sulfate-2'-palmitate (SL659).
CC       {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   -!- SIMILARITY: Belongs to the PapA acyltransferase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48295.1; -; Genomic_DNA.
DR   PIR; H70521; H70521.
DR   RefSeq; WP_003899707.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIK6; -.
DR   SMR; P9WIK6; -.
DR   EnsemblBacteria; AAK48295; AAK48295; MT3928.
DR   KEGG; mtc:MT3928; -.
DR   PATRIC; fig|83331.31.peg.4225; -.
DR   HOGENOM; CLU_034647_0_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..468
FT                   /note="Trehalose-2-sulfate acyltransferase PapA2"
FT                   /id="PRO_0000427990"
SQ   SEQUENCE   468 AA;  52150 MW;  9163239A6400DED9 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 LATLKPGT