LIPN_MYCTU
ID LIPN_MYCTU Reviewed; 376 AA.
AC P95125; F2GL39; I6Y254;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Carboxylic ester hydrolase LipN {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:26212120};
GN Name=lipN {ECO:0000312|EMBL:CCP45774.1};
GN OrderedLocusNames=Rv2970c {ECO:0000312|EMBL:CCP45774.1};
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] {ECO:0007744|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF TRP-145;
RP SER-216; ASP-316; ASP-320 AND HIS-346, AND ACTIVE SITE.
RX PubMed=26212120; DOI=10.1002/jcb.25285;
RA Jadeja D., Dogra N., Arya S., Singh G., Singh G., Kaur J.;
RT "Characterization of LipN (Rv2970c) of Mycobacterium tuberculosis H37Rv and
RT its probable role in xenobiotic degradation.";
RL J. Cell. Biochem. 117:390-401(2016).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=27690385; DOI=10.1021/acsinfecdis.6b00135;
RA Tallman K.R., Levine S.R., Beatty K.E.;
RT "Small-molecule probes reveal esterases with persistent activity in dormant
RT and reactivating Mycobacterium tuberculosis.";
RL ACS Infect. Dis. 2:936-944(2016).
CC -!- FUNCTION: Non specific carboxylic ester hydrolase. Hydrolyzes various
CC pNP-esters, with a preference for short carbon chain substrates. Can
CC also hydrolyze tributyrin to di- and monobutyrin and 4-
CC hydroxyphenylacetate to hydroquinone. {ECO:0000269|PubMed:26212120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308;
CC Evidence={ECO:0000269|PubMed:26212120};
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;
CC Evidence={ECO:0000269|PubMed:26212120};
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:26212120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC Evidence={ECO:0000269|PubMed:26212120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate +
CC H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658;
CC Evidence={ECO:0000269|PubMed:26212120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate
CC + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659;
CC Evidence={ECO:0000269|PubMed:26212120};
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:26212120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-acetoxyphenol + H2O = acetate + H(+) + hydroquinone;
CC Xref=Rhea:RHEA:47384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:30089, ChEBI:CHEBI:31128;
CC Evidence={ECO:0000269|PubMed:26212120};
CC -!- ACTIVITY REGULATION: Completely inhibited by tetrahydrolipstatin (THL),
CC RHC-80267 and N-bromosuccinimide. {ECO:0000269|PubMed:26212120}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=303 uM for pNP-butyrate {ECO:0000269|PubMed:26212120};
CC Note=kcat is 7283 min(-1) with pNP-butyrate as substrate.
CC {ECO:0000269|PubMed:26212120};
CC pH dependence:
CC Optimum pH is 8.0. Stable between pH 6.0-9.0 (with pNP-butyrate as
CC substrate). {ECO:0000269|PubMed:26212120};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius (with pNP-butyrate as
CC substrate). {ECO:0000269|PubMed:26212120};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26212120}.
CC -!- DEVELOPMENTAL STAGE: Remains active in dormant M.tuberculosis.
CC {ECO:0000269|PubMed:27690385}.
CC -!- INDUCTION: Expressed in macrophages after 6 hours of infection. In
CC vitro, expressed only in acidic stress conditions.
CC {ECO:0000269|PubMed:26212120}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP45774.1; -; Genomic_DNA.
DR RefSeq; NP_217486.1; NC_000962.3.
DR RefSeq; WP_003415015.1; NZ_NVQJ01000015.1.
DR AlphaFoldDB; P95125; -.
DR SMR; P95125; -.
DR STRING; 83332.Rv2970c; -.
DR ChEMBL; CHEMBL4105751; -.
DR SwissLipids; SLP:000001337; -.
DR ESTHER; myctu-Rv2970c; Hormone-sensitive_lipase_like.
DR PaxDb; P95125; -.
DR PRIDE; P95125; -.
DR DNASU; 887194; -.
DR GeneID; 45426959; -.
DR GeneID; 887194; -.
DR KEGG; mtu:Rv2970c; -.
DR PATRIC; fig|83332.111.peg.3309; -.
DR TubercuList; Rv2970c; -.
DR eggNOG; COG0657; Bacteria.
DR InParanoid; P95125; -.
DR OMA; QWLIYPR; -.
DR PhylomeDB; P95125; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..376
FT /note="Carboxylic ester hydrolase LipN"
FT /id="PRO_0000448853"
FT ACT_SITE 216
FT /evidence="ECO:0000305|PubMed:26212120"
FT ACT_SITE 316
FT /evidence="ECO:0000305|PubMed:26212120"
FT ACT_SITE 346
FT /evidence="ECO:0000305|PubMed:26212120"
FT MUTAGEN 145
FT /note="W->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26212120"
FT MUTAGEN 216
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26212120"
FT MUTAGEN 316
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26212120"
FT MUTAGEN 320
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:26212120"
FT MUTAGEN 346
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26212120"
SQ SEQUENCE 376 AA; 40135 MW; 3EC835B38B9003FC CRC64;
MTKSLPGVAD LRLGANHPRM WTRRVQGTVV NVGVKVLPWI PTPAKRILSA GRSVIIDGNT
LDPTLQLMLS TSRIFGVDGL AVDDDIVASR AHMRAICEAM PGPQIHVDVT DLSIPGPAGE
IPARHYRPSG GGATPLLVFY HGGGWTLGDL DTHDALCRLT CRDADIQVLS IDYRLAPEHP
APAAVEDAYA AFVWAHEHAS DEFGALPGRV AVGGDSAGGN LSAVVCQLAR DKARYEGGPT
PVLQWLLYPR TDFTAQTRSM GLFGNGFLLT KRDIDWFHTQ YLRDSDVDPA DPRLSPLLAE
SLSGLAPALI AVAGFDPLRD EGESYAKALR AAGTAVDLRY LGSLTHGFLN LFQLGGGSAA
GTNELISALR AHLSRV
