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   05-OCT-2016, entry version 28.
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.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, ENZYME REGULATION,
RP   MUTAGENESIS OF SER-87; ASP-192; ASP-217 AND HIS-240, ACTIVE SITE, AND
RP   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.,
RA   Singh K., Kaur J.;
RT   "Characterization of an acid inducible lipase Rv3203 from
RT   Mycobacterium 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
CC       shows significant activity with pNP-butyrate (68%), pNP-octanoate
CC       (82%), pNP-decanoate (90%), and pNP-laurate (74%). Is probably
CC       involved in lipid catabolism. Is active at low pH, and might play
CC       some important role in mycobacterial biology in macrophages where
CC       the bacteria encounters acidic stress.
CC       {ECO:0000269|PubMed:24234750}.
CC   -!- CATALYTIC ACTIVITY: A carboxylic ester + H(2)O = an alcohol + a
CC       carboxylate. {ECO:0000269|PubMed:24234750}.
CC   -!- ENZYME REGULATION: Is inbibited by tetrahydrolipstatin, a specific
CC       lipase inhibitor and RHC 80267, a diacylglycerol lipase inhibitor,
CC       but not by phenylglyoxal and iodoacetate.
CC       {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.
CC         The relative stability of purified enzyme is high at acidic pH
CC         and neutral pH (4.0-7.0) as compared to its relative stability
CC         at higher 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
CC       as compared to normal whereas no expression is observed under
CC       nutrient and oxidative stress conditions.
CC       {ECO:0000269|PubMed:24234750}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP46018.1; Type=Frameshift; Positions=38;
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; CCP46018.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; NP_217719.1; NC_000962.3.
DR   RefSeq; WP_003899968.1; NZ_KK339370.1.
DR   ProteinModelPortal; L0TC47; -.
DR   SMR; L0TC47; 4-260.
DR   STRING; 83332.Rv3203; -.
DR   SwissLipids; SLP:000001376; -.
DR   PaxDb; L0TC47; -.
DR   PRIDE; L0TC47; -.
DR   EnsemblBacteria; CCP46018; CCP46018; Rv3203.
DR   GeneID; 888133; -.
DR   KEGG; mtu:Rv3203; -.
DR   TubercuList; Rv3203; -.
DR   eggNOG; ENOG4108YIQ; Bacteria.
DR   eggNOG; ENOG4111KNX; LUCA.
DR   InParanoid; L0TC47; -.
DR   KO; K19311; -.
DR   BioCyc; MTBRV:RV3203-MONOMER; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR   GO; GO:0016298; F:lipase activity; IDA:UniProtKB.
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   Complete proteome; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Serine esterase.
FT   CHAIN         1    261       Lipase LipV.
FT                                /FTId=PRO_0000432515.
FT   ACT_SITE     87     87       Nucleophile.
FT                                {ECO:0000305|PubMed:24234750}.
FT   ACT_SITE    217    217       Charge relay system.
FT                                {ECO:0000305|PubMed:24234750}.
FT   ACT_SITE    240    240       Charge relay system.
FT                                {ECO:0000305|PubMed:24234750}.
FT   MUTAGEN      87     87       S->A: Loss of enzymatic activity.
FT                                {ECO:0000269|PubMed:24234750}.
FT   MUTAGEN     192    192       D->A: No effect on enzymatic activity.
FT                                {ECO:0000269|PubMed:24234750}.
FT   MUTAGEN     217    217       D->A: Loss of more than 70% enzymatic
FT                                activity. {ECO:0000269|PubMed:24234750}.
FT   MUTAGEN     240    240       H->A: Loss of enzymatic activity.
FT                                {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
//