LIPL_MYCTU
ID LIPL_MYCTU Reviewed; 429 AA.
AC P71778; I6X1F1; L0T9T1;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Esterase/beta-lactamase LipL {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:26672466};
DE EC=3.5.2.6 {ECO:0000269|PubMed:26672466};
GN Name=lipL {ECO:0000303|PubMed:26398213};
GN OrderedLocusNames=Rv1497 {ECO:0000312|EMBL:CCP44258.1};
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 AS AN ESTERASE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF GLY-49; GLY-50;
RP GLY-51; SER-88; LYS-91 AND SER-361.
RX PubMed=26398213; DOI=10.1371/journal.pone.0138151;
RA Cao J., Dang G., Li H., Li T., Yue Z., Li N., Liu Y., Liu S., Chen L.;
RT "Identification and characterization of lipase activity and immunogenicity
RT of LipL from Mycobacterium tuberculosis.";
RL PLoS ONE 10:E0138151-E0138151(2015).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, AND MUTAGENESIS OF SER-88; TYR-175; HIS-355 AND
RP SER-361.
RC STRAIN=H37Rv;
RX PubMed=26672466; DOI=10.1016/j.enzmictec.2015.10.007;
RA Singh G., Kumar A., Arya S., Gupta U.D., Singh K., Kaur J.;
RT "Characterization of a novel esterase Rv1497 of Mycobacterium tuberculosis
RT H37Rv demonstrating beta-lactamase activity.";
RL Enzyme Microb. Technol. 82:180-190(2016).
CC -!- FUNCTION: Shows both esterase and beta-lactamase activities, with a
CC much higher activity against phenyl esters than against beta-lactams
CC (PubMed:26398213, PubMed:26672466). Shows esterase activity against
CC both long-chain and short-chain p-nitrophenol (pNP) esters, with a
CC preference for shorter chain esters (PubMed:26398213, PubMed:26672466).
CC Hydrolyzes substrates containing beta-lactam ring such as nitrocefin
CC and ampicillin (PubMed:26672466). Functions as an immunogen that
CC activates both humoral and cell-mediated responses (PubMed:26398213).
CC {ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:26672466}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol
CC + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748;
CC Evidence={ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:26672466};
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:26398213, ECO:0000269|PubMed:26672466};
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:26398213, ECO:0000269|PubMed:26672466};
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:26398213, ECO:0000269|PubMed:26672466};
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:26672466};
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:26398213, ECO:0000269|PubMed:26672466};
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:26398213,
CC ECO:0000269|PubMed:26672466};
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:26398213,
CC ECO:0000269|PubMed:26672466};
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:26398213,
CC ECO:0000269|PubMed:26672466};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) +
CC hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656;
CC Evidence={ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000269|PubMed:26672466};
CC -!- ACTIVITY REGULATION: Esterase and beta-lactamase activities are
CC inhibited by the active site residue modifiers
CC phenylmethanesulfonylflouride (PMSF) and diethylpyrocarbonate (DEPC).
CC {ECO:0000269|PubMed:26672466}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.14 mM for pNP-butyrate {ECO:0000269|PubMed:26672466};
CC Note=kcat is 0.0932 sec(-1) with pNP-butyrate as substrate.
CC {ECO:0000269|PubMed:26672466};
CC pH dependence:
CC Optimum pH is 7.0 (with pNP-butyrate as substrate).
CC {ECO:0000269|PubMed:26672466};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius (with pNP-butyrate as
CC substrate). {ECO:0000269|PubMed:26672466};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:26398213}. Cell membrane
CC {ECO:0000269|PubMed:26398213}.
CC -!- INDUCTION: Up-regulated in acidic and oxidative stress conditions.
CC {ECO:0000269|PubMed:26672466}.
CC -!- SIMILARITY: Belongs to the beta-lactamase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44258.1; -; Genomic_DNA.
DR RefSeq; NP_216013.1; NC_000962.3.
DR RefSeq; WP_003407599.1; NZ_NVQJ01000004.1.
DR AlphaFoldDB; P71778; -.
DR SMR; P71778; -.
DR STRING; 83332.Rv1497; -.
DR SwissLipids; SLP:000001355; -.
DR PaxDb; P71778; -.
DR DNASU; 886575; -.
DR GeneID; 886575; -.
DR KEGG; mtu:Rv1497; -.
DR PATRIC; fig|83332.111.peg.1666; -.
DR TubercuList; Rv1497; -.
DR eggNOG; COG1680; Bacteria.
DR OMA; PMAFHLG; -.
DR PhylomeDB; P71778; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:MTBBASE.
DR GO; GO:0046503; P:glycerolipid catabolic process; IDA:MTBBASE.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Hydrolase; Membrane; Reference proteome;
KW Secreted.
FT CHAIN 1..429
FT /note="Esterase/beta-lactamase LipL"
FT /id="PRO_0000448854"
FT ACT_SITE 88
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D1"
FT MUTAGEN 49
FT /note="G->A: 70% loss of esterase activity."
FT /evidence="ECO:0000269|PubMed:26398213"
FT MUTAGEN 50
FT /note="G->A: 90% loss of esterase activity."
FT /evidence="ECO:0000269|PubMed:26398213"
FT MUTAGEN 51
FT /note="G->A: 60% loss of esterase activity."
FT /evidence="ECO:0000269|PubMed:26398213"
FT MUTAGEN 88
FT /note="S->A: Loss of esterase and beta-lactamase
FT activities."
FT /evidence="ECO:0000269|PubMed:26398213,
FT ECO:0000269|PubMed:26672466"
FT MUTAGEN 91
FT /note="K->A: 90% loss of esterase activity."
FT /evidence="ECO:0000269|PubMed:26398213"
FT MUTAGEN 175
FT /note="Y->A: Loss of esterase and beta-lactamase
FT activities."
FT /evidence="ECO:0000269|PubMed:26672466"
FT MUTAGEN 355
FT /note="H->A: 80% loss of esterase and beta-lactamase
FT activities."
FT /evidence="ECO:0000269|PubMed:26672466"
FT MUTAGEN 361
FT /note="S->A: Almost no change in esterase and beta-
FT lactamase activities."
FT /evidence="ECO:0000269|PubMed:26398213,
FT ECO:0000269|PubMed:26672466"
SQ SEQUENCE 429 AA; 45816 MW; D26C7F4100BE81CE CRC64;
MMVDTGVDHR AVSSHDGPDA GRRVFGAADP RFACVVRAFA SMFPGRRFGG GALAVYLDGQ
PVVDVWKGWA DRAGWVPWSA DSAPMVFSAT KGMTATVIHR LADRGLIDYE APVAEYWPAF
GANGKATLTV RDVMRHQAGL SGLRGATQQD LLDHVVMEER LAAAVPGRLL GKSAYHALTF
GWLMSGLARA VTGKDMRLLF REELAEPLDT DGLHLGRPPA DAPTRVAEII MPQDIAANAV
LTCAMRRLAH RFSGGFRSMY FPGAIAAVQG EAPLLDAEIP AANGVATARA LARMYGAIAN
GGEIDGIRFL SRELVTGLTR NRRQVLPDRN LLVPLNFHLG YHGMPIGNVM PGFGHVGLGG
SIGWTDPETG VAFALVHNRL LSPLVMTDHA GFVGIYHLIR QAAAQARKRG YQPVTPFGAP
YSEPGAAAG
