ID   TESA_MYCLE              Reviewed;         261 AA.
AC   Q9Z5K4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Thioesterase TesA {ECO:0000250|UniProtKB:P9WQD5};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:P9WQD5};
GN   Name=tesA; OrderedLocusNames=ML2359; ORFNames=MLCB12.04c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Involved in the synthesis of both phthiocerol dimycocerosates
CC       (PDIMs) and phenolic glycolipids (PGLs), which are structurally related
CC       lipids non-covalently bound to the outer cell wall layer of
CC       M.tuberculosis and are important virulence factors.
CC       {ECO:0000250|UniProtKB:P9WQD5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+);
CC         Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636;
CC         Evidence={ECO:0000250|UniProtKB:P9WQD5};
CC   -!- SIMILARITY: Belongs to the thioesterase family. {ECO:0000305}.
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DR   EMBL; AL035480; CAB36630.1; -; Genomic_DNA.
DR   EMBL; AL583925; CAC31875.1; -; Genomic_DNA.
DR   PIR; C87204; C87204.
DR   RefSeq; NP_302538.1; NC_002677.1.
DR   RefSeq; WP_010908858.1; NC_002677.1.
DR   AlphaFoldDB; Q9Z5K4; -.
DR   SMR; Q9Z5K4; -.
DR   STRING; 272631.ML2359; -.
DR   ESTHER; mycle-ML2359; Thioesterase.
DR   PRIDE; Q9Z5K4; -.
DR   EnsemblBacteria; CAC31875; CAC31875; CAC31875.
DR   KEGG; mle:ML2359; -.
DR   PATRIC; fig|272631.5.peg.4518; -.
DR   Leproma; ML2359; -.
DR   eggNOG; COG3208; Bacteria.
DR   HOGENOM; CLU_070456_1_2_11; -.
DR   OMA; FIHDEVE; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IEA:RHEA.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012223; TEII.
DR   InterPro; IPR001031; Thioesterase.
DR   PANTHER; PTHR11487; PTHR11487; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid biosynthesis; Lipid metabolism; Reference proteome;
KW   Virulence.
FT   CHAIN           1..261
FT                   /note="Thioesterase TesA"
FT                   /id="PRO_0000180367"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD5"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD5"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD5"
SQ   SEQUENCE   261 AA;  28950 MW;  C0BB07F88627F431 CRC64;
     MLHVLRPGYA GAVNGHSNNG NDDETSTTPT LYIFPHAGGD ATYYVPFSRE FSADIKRIAV
     HYPGQRDGYG LPALTSIPAL ADEIFAIMKP SAPPEGAVAF FGHSMGGMLA FEVALRFQSA
     GYRLIALFVS ACSAPGYIRY KQIKDFSDND MLDLVVRMTG MNPDFFEDEE FRVGVLPTLR
     AARIIAGYNC PPETTVSCPI YTYIGDKDWI ATQEDMKPWR ERTTGAFAIR VFPGDHFYLN
     GNLSELVCDI EDKTLEWCDR A