ID   PAPA2_MYCTA             Reviewed;         468 AA.
AC   A5U9E9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=MRA_3860;
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 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 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; ABQ75649.1; -; Genomic_DNA.
DR   RefSeq; WP_003899707.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U9E9; -.
DR   SMR; A5U9E9; -.
DR   STRING; 419947.MRA_3860; -.
DR   PRIDE; A5U9E9; -.
DR   EnsemblBacteria; ABQ75649; ABQ75649; MRA_3860.
DR   KEGG; mra:MRA_3860; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_034647_0_0_11; -.
DR   OMA; CMWVNRF; -.
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..468
FT                   /note="Trehalose-2-sulfate acyltransferase PapA2"
FT                   /id="PRO_0000314663"
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