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TESA_MYCTO
ID   TESA_MYCTO              Reviewed;         261 AA.
AC   P9WQD4; L0TBA2; P63460; Q10974;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Thioesterase TesA {ECO:0000250|UniProtKB:P9WQD5};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:P9WQD5};
GN   Name=tesA; OrderedLocusNames=MT2998;
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 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47325.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK47325.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70748; H70748.
DR   RefSeq; WP_003414828.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQD4; -.
DR   SMR; P9WQD4; -.
DR   ESTHER; myctu-yt28; Thioesterase.
DR   EnsemblBacteria; AAK47325; AAK47325; MT2998.
DR   KEGG; mtc:MT2998; -.
DR   PATRIC; fig|83331.31.peg.3238; -.
DR   HOGENOM; CLU_070456_1_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IEA:RHEA.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR012223; TEII.
DR   InterPro; IPR001031; Thioesterase.
DR   PANTHER; PTHR11487; PTHR11487; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid biosynthesis; Lipid metabolism; Virulence.
FT   CHAIN           1..261
FT                   /note="Thioesterase TesA"
FT                   /id="PRO_0000426795"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  29152 MW;  49FA9B32D8C636C2 CRC64;
     MLARHGPRYG GSVNGHSDDS SGDAKQAAPT LYIFPHAGGT AKDYVAFSRE FSADVKRIAV
     QYPGQHDRSG LPPLESIPTL ADEIFAMMKP SARIDDPVAF FGHSMGGMLA FEVALRYQSA
     GHRVLAFFVS ACSAPGHIRY KQLQDLSDRE MLDLFTRMTG MNPDFFTDDE FFVGALPTLR
     AVRAIAGYSC PPETKLSCPI YAFIGDKDWI ATQDDMDPWR DRTTEEFSIR VFPGDHFYLN
     DNLPELVSDI EDKTLQWHDR A
 
 
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