ID   LIPQ_MYCTU              Reviewed;         421 AA.
AC   I6Y9F7;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Esterase LipQ {ECO:0000305};
DE            EC=3.1.1.- {ECO:0000269|PubMed:26398213};
GN   Name=lipQ {ECO:0000312|EMBL:CCP45279.1};
GN   OrderedLocusNames=Rv2485c {ECO:0000312|EMBL:CCP45279.1};
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, AND CATALYTIC ACTIVITY.
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 IN VIRULENCE.
RX   PubMed=28412202; DOI=10.1016/j.micpath.2017.04.015;
RA   Kumar A., Manisha C., Sangha G.K., Shrivastava A., Kaur J.;
RT   "The immunosuppressive effects of a novel recombinant LipQ (Rv2485c)
RT   protein of Mycobacterium tuberculosis on human macrophage cell lines.";
RL   Microb. Pathog. 107:361-367(2017).
CC   -!- FUNCTION: Shows lipase activity (PubMed:26398213). Is highly
CC       immunogenic and may play an important role in the virulence and
CC       pathogenesis of M.tuberculosis infection, by altering the balance of
CC       cytokines. Significantly down-regulates the expression level of pro-
CC       inflammatory cytokines (TNF-alpha and IFN-gamma) and up-regulates the
CC       level of anti-inflammatory cytokines such as IL-4 and IL-10 as compared
CC       to LPS stimulated macrophages. Also inhibits the expression of iNOS,
CC       TLR2 and transcription factor NF-kappa-B in LPS stimulated macrophages
CC       whereas the expression of TLR-4 remains unchanged (PubMed:28412202).
CC       {ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:28412202}.
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   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45279.1; -; Genomic_DNA.
DR   RefSeq; NP_217001.1; NC_000962.3.
DR   RefSeq; WP_003412725.1; NZ_NVQJ01000067.1.
DR   AlphaFoldDB; I6Y9F7; -.
DR   SMR; I6Y9F7; -.
DR   STRING; 83332.Rv2485c; -.
DR   SwissLipids; SLP:000001357; -.
DR   ESTHER; myctu-Rv2485c; Hormone-sensitive_lipase_like.
DR   PaxDb; I6Y9F7; -.
DR   GeneID; 45426475; -.
DR   GeneID; 887876; -.
DR   KEGG; mtu:Rv2485c; -.
DR   PATRIC; fig|83332.111.peg.2781; -.
DR   TubercuList; Rv2485c; -.
DR   eggNOG; COG0657; Bacteria.
DR   OMA; TLMSRMV; -.
DR   PhylomeDB; I6Y9F7; -.
DR   PHI-base; PHI:7115; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome; Virulence.
FT   CHAIN           1..421
FT                   /note="Esterase LipQ"
FT                   /id="PRO_0000448881"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
FT   ACT_SITE        344
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
FT   ACT_SITE        377
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
SQ   SEQUENCE   421 AA;  45249 MW;  403CFFC586D8133E CRC64;
     MHIASVTSRC SRAGAEALRQ GAQLAADARD TCRAGALLLR GSPCAIGWVA GWLSAEFPAR
     VVTGHALSRI SPRSIGRFGT SWAAQRADQI LHAALVDAFG PDFRDLVWHP TGEQSEAARR
     SGLLNLPHIP GPHRRYAAQT SDIPYGPGGR ENLLDIWRRP DLAPGRRAPV LIQVPGGAWT
     INGKRPQAYP LMSRMVELGW ICVSINYSKS PRCTWPAHIV DVKRAIAWVR ENIADYGGDP
     DFITITGGSA GAHLAALAAL SANDPALQPG FESADTAVQA AAPYYGVYDL TNAENMHEMM
     MPFLEHFVMR SRYVDNPGLF KAASPISYVH SEAPPFFVLH GEKDPMVPSA QSRAFSAALR
     DAGAATVSYA ELPNAHHAFD LAATVRSRMV AEAVSDFLGV IYGRRMGARK GSLALSSPPA
     S