TESA_MYCBO
ID TESA_MYCBO Reviewed; 261 AA.
AC P63461; A0A1R3Y2M1; Q10974; X2BMI2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Thioesterase TesA {ECO:0000250|UniProtKB:P9WQD5};
DE EC=3.1.2.- {ECO:0000250|UniProtKB:P9WQD5};
GN Name=tesA; OrderedLocusNames=BQ2027_MB2953;
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: 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; LT708304; SIU01574.1; -; Genomic_DNA.
DR RefSeq; NP_856598.1; NC_002945.3.
DR RefSeq; WP_003414828.1; NC_002945.4.
DR AlphaFoldDB; P63461; -.
DR SMR; P63461; -.
DR ESTHER; myctu-yt28; Thioesterase.
DR EnsemblBacteria; SIU01574; SIU01574; BQ2027_MB2953.
DR PATRIC; fig|233413.5.peg.3240; -.
DR OMA; FIHDEVE; -.
DR Proteomes; UP000001419; 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_0000180366"
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