ID   PAPA3_MYCTO             Reviewed;         472 AA.
AC   P9WIK4; F2GG06; L0T8W4; O50438; Q7D8P1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Acyltransferase PapA3 {ECO:0000250|UniProtKB:P9WIK5};
DE            EC=2.3.1.278 {ECO:0000250|UniProtKB:P9WIK5};
DE            EC=2.3.1.279 {ECO:0000250|UniProtKB:P9WIK5};
DE   AltName: Full=Long-chain-acyl-CoA--trehalose acyltransferase {ECO:0000250|UniProtKB:P9WIK5};
DE   AltName: Full=Mycolipenoyl-CoA--2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase {ECO:0000250|UniProtKB:P9WIK5};
DE   AltName: Full=Polyketide synthase-associated protein A3;
GN   Name=papA3; OrderedLocusNames=MT1219;
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: Involved in the biosynthesis of polyacyltrehalose (PAT), a
CC       pentaacylated, trehalose-based glycolipid that could have a role in
CC       anchoring the bacterial capsule. Catalyzes the sequential transfer of
CC       two palmitoyl groups onto a single glucose residue of trehalose
CC       generating the diacylated product 2,3-diacyltrehalose (trehalose
CC       dipalmitate). {ECO:0000250|UniProtKB:P9WIK5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acyl-CoA + alpha,alpha-trehalose = 2-O-
CC         (long-chain fatty acyl)-alpha,alpha-trehalose + CoA;
CC         Xref=Rhea:RHEA:58044, ChEBI:CHEBI:16551, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:142477; EC=2.3.1.279;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58045;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-O-(long-chain fatty acyl)-alpha,alpha-trehalose + a
CC         mycolipenoyl-CoA = 2-O-(long-chain fatty acyl)-3-O-mycolipenoyl-
CC         trehalose + CoA; Xref=Rhea:RHEA:38459, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:142475, ChEBI:CHEBI:142476, ChEBI:CHEBI:142477;
CC         EC=2.3.1.278; Evidence={ECO:0000250|UniProtKB:P9WIK5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38460;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + hexadecanoyl-CoA = 2-O-hexadecanoyl-
CC         alpha,alpha-trehalose + CoA; Xref=Rhea:RHEA:44052, ChEBI:CHEBI:16551,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:84041;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44053;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-O-hexadecanoyl-alpha,alpha-trehalose + hexadecanoyl-CoA = 2-
CC         O,3-O-dihexadecanoyl-alpha,alpha-trehalose + CoA;
CC         Xref=Rhea:RHEA:44056, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:84041, ChEBI:CHEBI:84042;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44057;
CC         Evidence={ECO:0000250|UniProtKB:P9WIK5};
CC   -!- SIMILARITY: Belongs to the PapA acyltransferase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45476.1; -; Genomic_DNA.
DR   PIR; F70876; F70876.
DR   RefSeq; WP_003898759.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIK4; -.
DR   SMR; P9WIK4; -.
DR   EnsemblBacteria; AAK45476; AAK45476; MT1219.
DR   GeneID; 45425153; -.
DR   KEGG; mtc:MT1219; -.
DR   PATRIC; fig|83331.31.peg.1318; -.
DR   HOGENOM; CLU_034647_0_0_11; -.
DR   Proteomes; UP000001020; 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..472
FT                   /note="Acyltransferase PapA3"
FT                   /id="PRO_0000427991"
SQ   SEQUENCE   472 AA;  51575 MW;  CAA4CB55B9B7C812 CRC64;
     MLRVGPLTIG TLDDWAPSTG STVSWRPSAV AHTKASQAPI SDVPVSYMQA QHIRGYCEQK
     AKGLDYSRLM VVSCQQPGQC DIRAANYVIN AHLRRHDTYR SWFQYNGNGQ IIRRTIQDPA
     DIEFVPVHHG ELTLPQIREI VQNTPDPLQW GCFRFGIVQG CDHFTFFASV DHVHVDAMIV
     GVTLMEFHLM YAALVGGHAP LELPPAGSYD DFCRRQHTFS STLTVESPQV RAWTKFAEGT
     NGSFPDFPLP LGDPSKPSDA DIVTVMMLDE EQTAQFESVC TAAGARFIGG VLACCGLAEH
     ELTGTTTYYG LTPRDTRRTP ADAMTQGWFT GLIPITVPIA GSAFGDAARA AQTSFDSGVK
     LAEVPYDRVV ELSSTLTMPR PNFPVVNFLD AGAAPLSVLL TAELTGTNIG VYSDGRYSYQ
     LSIYVIRVEQ GTAVAVMFPD NPIARESVAR YLATLKSVFQ RVAESGQQQN VA