LIPV_MYCTU
ID LIPV_MYCTU Reviewed; 261 AA.
AC L0TC47;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Lipase LipV {ECO:0000303|PubMed:24234750};
DE EC=3.1.1.1 {ECO:0000269|PubMed:24234750};
GN Name=lipV {ECO:0000303|PubMed:24234750};
GN OrderedLocusNames=Rv3203 {ECO:0000312|EMBL:CCP46018.1};
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 PROTEIN SEQUENCE OF 18-29, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SEQUENCE
RP REVISION TO N-TERMINUS.
RC STRAIN=ATCC 25618 / H37Rv;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, ACTIVITY REGULATION, MUTAGENESIS OF SER-87; ASP-192;
RP ASP-217 AND HIS-240, ACTIVE SITE, AND 3D-STRUCTURE MODELING.
RC STRAIN=H37Ra, and H37Rv;
RX PubMed=24234750; DOI=10.1007/s11033-013-2861-3;
RA Singh G., Arya S., Narang D., Jadeja D., Singh G., Gupta U.D., Singh K.,
RA Kaur J.;
RT "Characterization of an acid inducible lipase Rv3203 from Mycobacterium
RT tuberculosis H37Rv.";
RL Mol. Biol. Rep. 41:285-296(2014).
CC -!- FUNCTION: Lipase that displays broad substrate specificity and
CC preferentially hydrolyzes p-nitrophenyl myristate in vitro. Also shows
CC significant activity with pNP-butyrate (68%), pNP-octanoate (82%), pNP-
CC decanoate (90%), and pNP-laurate (74%). Is probably involved in lipid
CC catabolism. Is active at low pH, and might play some important role in
CC mycobacterial biology in macrophages where the bacteria encounters
CC acidic stress. {ECO:0000269|PubMed:24234750}.
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; EC=3.1.1.1;
CC Evidence={ECO:0000269|PubMed:24234750};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:24234750};
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:24234750};
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:24234750};
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:24234750};
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:24234750};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:24234750};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoate ester = an aliphatic alcohol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:47396, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:75925; Evidence={ECO:0000269|PubMed:24234750};
CC -!- ACTIVITY REGULATION: Is inbibited by tetrahydrolipstatin, a specific
CC lipase inhibitor and RHC 80267, a diacylglycerol lipase inhibitor, but
CC not by phenylglyoxal and iodoacetate. {ECO:0000269|PubMed:24234750}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=714.28 uM for pNP-myristate {ECO:0000269|PubMed:24234750};
CC Note=kcat is 1312 sec(-1) with pNP-myristate as substrate.
CC {ECO:0000269|PubMed:24234750};
CC pH dependence:
CC Optimum pH is 8.0. Retains nearly 60% enzyme activity at pH 6.0. The
CC relative stability of purified enzyme is high at acidic pH and
CC neutral pH (4.0-7.0) as compared to its relative stability at higher
CC pH (9.0-10.0). {ECO:0000269|PubMed:24234750};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:24234750};
CC -!- INDUCTION: Expression is early up-regulated during acidic stress as
CC compared to normal whereas no expression is observed under nutrient and
CC oxidative stress conditions. {ECO:0000269|PubMed:24234750}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP46018.1; Type=Frameshift; Evidence={ECO:0000305|PubMed:21969609, ECO:0000305|PubMed:34915127};
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DR EMBL; AL123456; CCP46018.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; NP_217719.1; NC_000962.3.
DR RefSeq; WP_003899968.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; L0TC47; -.
DR STRING; 83332.Rv3203; -.
DR SwissLipids; SLP:000001376; -.
DR ESTHER; myctu-lipv; 6_AlphaBeta_hydrolase.
DR PaxDb; L0TC47; -.
DR DNASU; 888133; -.
DR GeneID; 888133; -.
DR KEGG; mtu:Rv3203; -.
DR PATRIC; fig|83332.12.peg.3582; -.
DR TubercuList; Rv3203; -.
DR eggNOG; COG0596; Bacteria.
DR InParanoid; L0TC47; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0016298; F:lipase activity; IDA:UniProtKB.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Serine esterase.
FT CHAIN 1..261
FT /note="Lipase LipV"
FT /id="PRO_0000432515"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:24234750"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:24234750"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:24234750"
FT MUTAGEN 87
FT /note="S->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24234750"
FT MUTAGEN 192
FT /note="D->A: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24234750"
FT MUTAGEN 217
FT /note="D->A: Loss of more than 70% enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24234750"
FT MUTAGEN 240
FT /note="H->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24234750"
SQ SEQUENCE 261 AA; 27868 MW; 37AC9C780CCF9E29 CRC64;
MIIDLHVQRY GPSGPARVLT IHGVTEHGRI WHRLAHHLPE IPIAAPDLLG HGRSPWAAPW
TIDANVSALA ALLDNQGDGP VVVVGHSFGG AVAMHLAAAR PDQVAALVLL DPAVALDGSR
VREVVDAMLA SPDYLDPAEA RAEKATGAWA DVDPPVLDAE LDEHLVALPN GRYGWRISLP
AMVCYWSELA RDIVLPPVGT ATTLVRAVRA SPAYVSDQLL AALDKRLGAD FELLDFDCGH
MVPQAKPTEV AAVIRSRLGP R
