ID   TESA_MYCMM              Reviewed;         249 AA.
AC   B2HIN3;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Thioesterase TesA {ECO:0000305};
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:P9WQD5};
GN   Name=tesA {ECO:0000303|PubMed:21592957};
GN   OrderedLocusNames=MMAR_1778 {ECO:0000312|EMBL:ACC40227.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-92.
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=21592957; DOI=10.1074/jbc.m111.247601;
RA   Chavadi S.S., Edupuganti U.R., Vergnolle O., Fatima I., Singh S.M.,
RA   Soll C.E., Quadri L.E.;
RT   "Inactivation of tesA reduces cell wall lipid production and increases drug
RT   susceptibility in mycobacteria.";
RL   J. Biol. Chem. 286:24616-24625(2011).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21375593; DOI=10.1111/j.1365-2958.2011.07618.x;
RA   Alibaud L., Rombouts Y., Trivelli X., Burguiere A., Cirillo S.L.,
RA   Cirillo J.D., Dubremetz J.F., Guerardel Y., Lutfalla G., Kremer L.;
RT   "A Mycobacterium marinum TesA mutant defective for major cell wall-
RT   associated lipids is highly attenuated in Dictyostelium discoideum and
RT   zebrafish embryos.";
RL   Mol. Microbiol. 80:919-934(2011).
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:0000269|PubMed:21375593, ECO:0000269|PubMed:21592957}.
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   -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to a drastic reduction
CC       in PDIM and PGL production (PubMed:21592957, PubMed:21375593). Mutant
CC       shows increased susceptibility to several antibiotics (PubMed:21592957,
CC       PubMed:21375593). Mutant is highly attenuated when injected into the
CC       zebrafish embryo bloodstream, but virulence is retained when bacteria
CC       are injected into the notochord (PubMed:21375593). Deletion leads to an
CC       increase in growth yield in vitro (PubMed:21592957).
CC       {ECO:0000269|PubMed:21375593, ECO:0000269|PubMed:21592957}.
CC   -!- SIMILARITY: Belongs to the thioesterase family. {ECO:0000305}.
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DR   EMBL; CP000854; ACC40227.1; -; Genomic_DNA.
DR   RefSeq; WP_011740081.1; NC_010612.1.
DR   AlphaFoldDB; B2HIN3; -.
DR   SMR; B2HIN3; -.
DR   STRING; 216594.MMAR_1778; -.
DR   EnsemblBacteria; ACC40227; ACC40227; MMAR_1778.
DR   KEGG; mmi:MMAR_1778; -.
DR   eggNOG; COG3208; Bacteria.
DR   HOGENOM; CLU_070456_1_2_11; -.
DR   OMA; FIHDEVE; -.
DR   OrthoDB; 1119700at2; -.
DR   BioCyc; MetaCyc:MON-19643; -.
DR   Proteomes; UP000001190; 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   1: Evidence at protein level;
KW   Hydrolase; Lipid biosynthesis; Lipid metabolism; Reference proteome;
KW   Virulence.
FT   CHAIN           1..249
FT                   /note="Thioesterase TesA"
FT                   /id="PRO_0000448708"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000305|PubMed:21592957"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD5"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD5"
FT   MUTAGEN         92
FT                   /note="S->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:21592957"
SQ   SEQUENCE   249 AA;  27601 MW;  9A7A33942FB991E3 CRC64;
     MNGRSSNSKS DEKLTAPTLY IFPHAGGTAK DYVPFAKEFS GEVKRVAVQY PGQQDGYGLP
     PLESIPGLAE EIFAIMKPAA RIDTPVALFG HSMGGMLAFE VALRFEAAGY RVLALFLSAC
     SAPGHIKYKQ LKGYSDNEML DLVARATGTD PEFFNDEEFR VGVLPTLRAV RAIAGYSCPP
     ENKLSCPIYT FIGSKDWIAT REDMEPWRER TTGDFSLREF PGDHFYLNKN LPELVSDIEI
     GTLQQFDQI