LIPF_MYCTO
ID LIPF_MYCTO Reviewed; 373 AA.
AC Q7D5F9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Carboxylesterase/phospholipase LipF {ECO:0000250|UniProtKB:O06350, ECO:0000303|PubMed:12218036};
DE EC=3.1.1.1 {ECO:0000250|UniProtKB:O06350};
DE EC=3.1.4.3 {ECO:0000250|UniProtKB:O06350};
GN Name=lipF {ECO:0000303|PubMed:12218036};
GN OrderedLocusNames=MT3591 {ECO:0000312|EMBL:AAK47950.1};
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP INDUCTION BY ACID.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12595455; DOI=10.1128/iai.71.3.1379-1388.2003;
RA Saviola B., Woolwine S.C., Bishai W.R.;
RT "Isolation of acid-inducible genes of Mycobacterium tuberculosis with the
RT use of recombinase-based in vivo expression technology.";
RL Infect. Immun. 71:1379-1388(2003).
RN [3]
RP INDUCTION BY ACID, AND IDENTIFICATION OF PROMOTER.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=17434691; DOI=10.1016/j.gene.2006.12.037;
RA Richter L., Tai W., Felton J., Saviola B.;
RT "Determination of the minimal acid-inducible promoter region of the lipF
RT gene from Mycobacterium tuberculosis.";
RL Gene 395:22-28(2007).
RN [4]
RP INDUCTION BY ACID.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=17869077; DOI=10.1016/j.micres.2007.06.003;
RA Richter L., Saviola B.;
RT "The lipF promoter of Mycobacterium tuberculosis is upregulated
RT specifically by acidic pH but not by other stress conditions.";
RL Microbiol. Res. 164:228-232(2009).
CC -!- FUNCTION: A short-chain esterase and phospholipase.
CC {ECO:0000250|UniProtKB:O06350}.
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:0000250|UniProtKB:O06350};
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:0000250|UniProtKB:O06350};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605;
CC Evidence={ECO:0000250|UniProtKB:O06350};
CC -!- INDUCTION: Induced by acidic conditions (PubMed:12595455,
CC PubMed:17434691). Induction levels are the same at pH 4.5 and pH 5.0
CC and decrease as the pH approaches 6.4. No induction is seen at higher
CC pH, nor by oxidative, hypoxic or temperature stress (PubMed:17869077).
CC Induction is maximal after 22 hours exposure to acid. Induction does
CC not depend on sigF, and does not seem to occur in activated murine
CC macrophages (PubMed:12595455). {ECO:0000269|PubMed:12595455,
CC ECO:0000269|PubMed:17434691, ECO:0000269|PubMed:17869077}.
CC -!- MISCELLANEOUS: The acid-inducible promoter is found 515 bases upstream
CC of the predicted start site. Three start sites have been proposed for
CC this protein, Met-1, Met-47 and Val-97, this is the longest
CC translation, there is protein sequence (for strain H37Rv) that suggests
CC Met-1 is the correct start. {ECO:0000269|PubMed:17434691}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK47950.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:O06350};
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DR EMBL; AE000516; AAK47950.1; ALT_INIT; Genomic_DNA.
DR ESTHER; myctu-Rv3487c; Hormone-sensitive_lipase_like.
DR EnsemblBacteria; AAK47950; AAK47950; MT3591.
DR KEGG; mtc:MT3591; -.
DR HOGENOM; CLU_012494_13_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Hydrolase; Serine esterase.
FT CHAIN 1..373
FT /note="Carboxylesterase/phospholipase LipF"
FT /id="PRO_0000455445"
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:0000250|UniProtKB:O06350"
FT ACT_SITE 285
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 315
FT /evidence="ECO:0000250|UniProtKB:O06350"
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
