PAPA2_MYCBO
ID PAPA2_MYCBO Reviewed; 468 AA.
AC Q7TVL3; A0A1R3Y5A5; X2BPC4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=BQ2027_MB3850C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU02479.1; -; Genomic_DNA.
DR RefSeq; NP_857487.1; NC_002945.3.
DR RefSeq; WP_010950943.1; NC_002945.4.
DR AlphaFoldDB; Q7TVL3; -.
DR SMR; Q7TVL3; -.
DR EnsemblBacteria; SIU02479; SIU02479; BQ2027_MB3850C.
DR PATRIC; fig|233413.5.peg.4210; -.
DR OMA; CMWVNRF; -.
DR Proteomes; UP000001419; 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_0000314660"
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