GDSLL_MYCTU
ID GDSLL_MYCTU Reviewed; 314 AA.
AC O53423; I6X087; L0T5R9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=GDSL-like esterase Rv1075c {ECO:0000305};
DE EC=3.1.-.- {ECO:0000269|PubMed:31001637};
DE AltName: Full=Acetylesterase {ECO:0000305};
DE EC=3.1.1.6 {ECO:0000269|PubMed:31001637};
DE Flags: Precursor;
GN OrderedLocusNames=Rv1075c {ECO:0000312|EMBL:CCP43826.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-80;
RP ASP-244 AND HIS-247.
RC STRAIN=CDC 1551 / Oshkosh, and H37Rv;
RX PubMed=31001637; DOI=10.1093/infdis/jiz169;
RA Yang D., He X., Li S., Liu J., Stabenow J., Zalduondo L., White S.,
RA Kong Y.;
RT "Rv1075c of Mycobacterium tuberculosis is a GDSL-like esterase and is
RT important for intracellular survival.";
RL J. Infect. Dis. 220:676-686(2019).
CC -!- FUNCTION: Esterase that preferentially hydrolyzes short-chain fatty
CC acids, particularly pNP-acetate (C2) and pNP-butyrate (C4). Has also
CC weak activity with pNP-hexanoate (C6) and pNP-octanoate (C8). It can
CC also hydrolyze short-chain tryglycerides such as triacetin and
CC tributyrin (PubMed:31001637). Important for intracellular survival
CC (PubMed:31001637). {ECO:0000269|PubMed:31001637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6;
CC Evidence={ECO:0000269|PubMed:31001637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:31001637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + triacetin = acetate + diacetylglycerol + H(+);
CC Xref=Rhea:RHEA:48028, ChEBI:CHEBI:9661, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:88156;
CC Evidence={ECO:0000269|PubMed:31001637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:31001637};
CC -!- ACTIVITY REGULATION: Esterase activity is significantly inhibited by
CC the serine modifier phenylmethylsulfonyl fluoride (PMSF). Completely
CC inhibited by diethyl pyrocarbonate. {ECO:0000269|PubMed:31001637}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=753 uM for pNP-acetate {ECO:0000269|PubMed:31001637};
CC pH dependence:
CC Optimum pH is 9.0 (with pNP-acetate as substrate).
CC {ECO:0000269|PubMed:31001637};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius (with pNP-acetate as
CC substrate). {ECO:0000269|PubMed:31001637};
CC -!- INDUCTION: Induced under acidic conditions.
CC {ECO:0000269|PubMed:31001637}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene leads to significantly
CC reduced bacterial growth in macrophages and in mice.
CC {ECO:0000269|PubMed:31001637}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43826.1; -; Genomic_DNA.
DR RefSeq; NP_215591.1; NC_000962.3.
DR RefSeq; WP_003405726.1; NZ_NVQJ01000072.1.
DR AlphaFoldDB; O53423; -.
DR STRING; 83332.Rv1075c; -.
DR PaxDb; O53423; -.
DR PRIDE; O53423; -.
DR DNASU; 887110; -.
DR GeneID; 45425047; -.
DR GeneID; 887110; -.
DR KEGG; mtu:Rv1075c; -.
DR PATRIC; fig|83332.111.peg.1197; -.
DR TubercuList; Rv1075c; -.
DR eggNOG; COG2755; Bacteria.
DR OMA; NDVTHRM; -.
DR PhylomeDB; O53423; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008126; F:acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..314
FT /note="GDSL-like esterase Rv1075c"
FT /id="PRO_0000448307"
FT REGION 276..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT SITE 119
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT SITE 149
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT MUTAGEN 80
FT /note="S->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:31001637"
FT MUTAGEN 244
FT /note="D->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:31001637"
FT MUTAGEN 247
FT /note="H->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:31001637"
SQ SEQUENCE 314 AA; 32879 MW; FC20DF4ADA6D1C33 CRC64;
MPRRSTIALA TAGALASTGT AYLGARNLLV GQATHARTVI PKSFDAPPRA DGVYTRGGGP
VQRWRREVPF DVHLMIFGDS TATGYGCASA EEVPGVLIAR GLAEQTGKRI RLSTKAIVGA
TSKGVCGQVD AMFVVGPPPD AAVIMIGAND ITALNGIGPS AQRLADCVRR LRTRGAVVVV
GTCPDLGVIT AIPQPLRALA HTRGVRLARA QTAAVKAAGG VPVPLGHLLA PKFRAMPELM
FSADRYHPSA PAYALAADLL FLALRDALTE KLDIPIHETP SRPGTATLEP GHTRHSMMSR
LRRPRPARAV PTGG
