LIPF_MYCTU
ID LIPF_MYCTU Reviewed; 373 AA.
AC O06350; F2GJ51; L0TCW1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 4.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Carboxylesterase/phospholipase LipF {ECO:0000303|PubMed:15939293, ECO:0000303|PubMed:18535356};
DE EC=3.1.1.1 {ECO:0000269|PubMed:15939293};
DE EC=3.1.4.3 {ECO:0000269|PubMed:18535356};
DE Flags: Precursor;
GN Name=lipF; OrderedLocusNames=Rv3487c;
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 8-39 AND 85-98, 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 PROTEIN SEQUENCE OF 85-98, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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., 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 DISRUPTION PHENOTYPE.
RC STRAIN=Mt103;
RX PubMed=10564470; DOI=10.1046/j.1365-2958.1999.01593.x;
RA Camacho L.R., Ensergueix D., Perez E., Gicquel B., Guilhot C.;
RT "Identification of a virulence gene cluster of Mycobacterium tuberculosis
RT by signature-tagged transposon mutagenesis.";
RL Mol. Microbiol. 34:257-267(1999).
RN [5]
RP FUNCTION AS A CARBOXYLESTERASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, AND MUTAGENESIS OF SER-186; GLU-285 AND HIS-315.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15939293; DOI=10.1016/j.pep.2005.03.022;
RA Zhang M., Wang J.D., Li Z.F., Xie J., Yang Y.P., Zhong Y., Wang H.H.;
RT "Expression and characterization of the carboxyl esterase Rv3487c from
RT Mycobacterium tuberculosis.";
RL Protein Expr. Purif. 42:59-66(2005).
RN [6]
RP FUNCTION AS A PHOSPHOLIPASE, CATALYTIC ACTIVITY, AND POSSIBLE SUBCELLULAR
RP LOCATION.
RX PubMed=18535356; DOI=10.1007/s12038-008-0039-2;
RA Srinivas M., Rajakumari S., Narayana Y., Joshi B., Katoch V.M.,
RA Rajasekharan R., Balaji K.N.;
RT "Functional characterization of the phospholipase C activity of Rv3487c and
RT its localization on the cell wall of Mycobacterium tuberculosis.";
RL J. Biosci. 33:221-230(2008).
CC -!- FUNCTION: Hydrolyzes short-chain esters. Shows maximal activity with
CC triacetin and p-nitrophenyl acetate. Has no enzyme activity on
CC triacylglycerides or p-nitrophenyl esters (p-NP) with long fatty acids
CC (tricaprin, p-NP caprylate, or p-NP caprate); experiments performed
CC with enzyme missing the first 97 residues (PubMed:15939293). Has
CC phospholipase C activity, making 1,2-DAG phosphocholine; experiments
CC performed with enzyme missing the first 97 residues (PubMed:18535356).
CC {ECO:0000269|PubMed:15939293, ECO:0000269|PubMed:18535356}.
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:15939293};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC Evidence={ECO:0000269|PubMed:18535356};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605;
CC Evidence={ECO:0000269|PubMed:18535356};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for triacetin {ECO:0000269|PubMed:15939293};
CC KM=0.24 mM for tributyrin {ECO:0000269|PubMed:15939293};
CC KM=0.25 mM for tricaproin {ECO:0000269|PubMed:15939293};
CC KM=1.46 mM for tricaprylin {ECO:0000269|PubMed:15939293};
CC KM=0.16 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:15939293};
CC KM=0.18 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:15939293};
CC KM=0.58 mM for p-nitrophenyl caproate {ECO:0000269|PubMed:15939293};
CC Note=kcat is 581.2 sec(-1) for triacetin. kcat is 223.7 sec(-1) for
CC tributyrin. kcat is 122.9 sec(-1) for tricaproin. kcat is 15.6 sec(-
CC 1) for tricaprylin. kcat is 501.8 sec(-1) for p-nitrophenyl acetate.
CC kcat is 119.7 sec(-1) for p-nitrophenyl butyrate. kcat is 33.1 sec(-
CC 1) for p-nitrophenyl caproate. {ECO:0000269|PubMed:15939293};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:15939293};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:15939293};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000305|PubMed:18535356}. Note=Detected by antibodies in a wild-
CC type strain and upon expression of a probably truncated form in
CC M.smegmatis. {ECO:0000269|PubMed:18535356}.
CC -!- INDUCTION: Induced by acidic pH. {ECO:0000269|PubMed:15939293}.
CC -!- DISRUPTION PHENOTYPE: Mutants show reduced ability to grow in a mouse
CC lung. {ECO:0000269|PubMed:10564470}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: Experiments to characterize enzymatic activity in
CC (PubMed:21969609) and (PubMed:10564470) were performed with protein
CC overexpressed in E.coli or M.smegmatis respectively; both papers use a
CC protein that starts on Val-97 (PubMed:15939293, PubMed:18535356). Three
CC start sites have been proposed for this protein, Met-1, Met-47 and Val-
CC 97, this is the longest translation. There is protein sequence that
CC suggests Met-1 is the correct start. Antibodies detect a protein larger
CC than 38 kDa in M.tuberculosis (PubMed:18535356).
CC {ECO:0000269|PubMed:15939293, ECO:0000269|PubMed:18535356,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP46309.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP46309.1; ALT_INIT; Genomic_DNA.
DR PIR; D70569; D70569.
DR RefSeq; NP_218004.3; NC_000962.3.
DR RefSeq; WP_003418946.1; NC_000962.3.
DR AlphaFoldDB; O06350; -.
DR SMR; O06350; -.
DR STRING; 83332.Rv3487c; -.
DR ESTHER; myctu-Rv3487c; Hormone-sensitive_lipase_like.
DR PaxDb; O06350; -.
DR GeneID; 888430; -.
DR KEGG; mtu:Rv3487c; -.
DR TubercuList; Rv3487c; -.
DR eggNOG; COG0657; Bacteria.
DR InParanoid; O06350; -.
DR OMA; ATCSLRQ; -.
DR PhylomeDB; O06350; -.
DR BRENDA; 3.1.4.3; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:MTBBASE.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:RHEA.
DR GO; GO:0004629; F:phospholipase C activity; IDA:MTBBASE.
DR GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0010447; P:response to acidic pH; IEP:MTBBASE.
DR GO; GO:0052572; P:response to host immune response; IMP:MTBBASE.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Hydrolase; Reference proteome;
KW Secreted; Serine esterase; Stress response.
FT PROPEP 1..7
FT /evidence="ECO:0000269|PubMed:34915127"
FT /id="PRO_0000455443"
FT CHAIN 8..373
FT /note="Carboxylesterase/phospholipase LipF"
FT /id="PRO_0000419168"
FT MOTIF 116..118
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 186
FT /evidence="ECO:0000305|PubMed:15939293"
FT ACT_SITE 285
FT /evidence="ECO:0000305|PubMed:15939293"
FT ACT_SITE 315
FT /evidence="ECO:0000305|PubMed:15939293"
FT MUTAGEN 186
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15939293"
FT MUTAGEN 285
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15939293"
FT MUTAGEN 315
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15939293"
SQ SEQUENCE 373 AA; 39611 MW; D7CBF9C9A49405F0 CRC64;
MSSYYARRPL QSSGCSNSDS CWDGAPIEIT ESGPSVAGRL AALASRMTIK PLMTVGSYLS
PLPLPLGFVD FACRVWRPGQ GTVRTTINLP NATAQLVRAP GVRAADGAGR VVLYLHGGAF
VMCGPNSHSR IVNALSGFAE SPVLIVDYRL IPKHSLGMAL DDCHDAYQWL RARGYRPEQI
VLAGDSAGGY LALALAQRLQ CDDEKPAAIV AISPLLQLAK GPKQDHPNIG TDAMFPARAF
DALAAWVRAA AAKNMVDGRP EDLYEPLDHI ESSLPPTLIH VSGSEVLLHD AQLGAGKLAA
AGVCAEVRVW PGQAHLFQLA TPLVPEATRS LRQIGQFIRD ATADSSLSPV HRSRYVAGSP
RAASRGAFGQ SPI
