ID   LIPR_MYCTO              Reviewed;         308 AA.
AC   P9WK84; F2GNY4; L0TEI3; O53301; Q7D657;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Putative acetyl-hydrolase LipR;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=lipR; Synonyms=bah; OrderedLocusNames=MT3169;
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).
CC   -!- FUNCTION: Required for maintaining the appropriate mycolic acid
CC       composition and permeability of the envelope on its exposure to acidic
CC       pH. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47505.1; -; Genomic_DNA.
DR   PIR; H70852; H70852.
DR   RefSeq; WP_003901538.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK84; -.
DR   SMR; P9WK84; -.
DR   ESTHER; myctu-Rv3084; Hormone-sensitive_lipase_like.
DR   EnsemblBacteria; AAK47505; AAK47505; MT3169.
DR   KEGG; mtc:MT3169; -.
DR   PATRIC; fig|83331.31.peg.3415; -.
DR   HOGENOM; CLU_012494_13_1_11; -.
DR   Proteomes; UP000001020; 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   3: Inferred from homology;
KW   Hydrolase; Signal.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..308
FT                   /note="Putative acetyl-hydrolase LipR"
FT                   /id="PRO_0000427698"
FT   MOTIF           76..78
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        146
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
SQ   SEQUENCE   308 AA;  32617 MW;  8F9938336F47BAE7 CRC64;
     MNLRKNVIRS VLRGARPLFA SRRLGIAGRR VLLATLTAGA RAPKGTRFQR VSIAGVPVQR
     VQPPHAATSG TLIYLHGGAY ALGSARGYRG LAAQLAAAAG MTALVPDYTR APHAHYPVAL
     EEMAAVYTRL LDDGLDPKTT VIAGDSAGGG LTLALAMALR DRGIQAPAAL GLICPWADLA
     VDIEATRPAL RDPLILPSMC TEWAPRYVGS SDPRLPGISP VYGDMSGLPP IVMQTAGDDP
     ICVDADKIET ACAASKTSIE HRRFAGMWHD FHLQVSLLPE ARDAIADLGA RLRGHLHQSQ
     GQPRGVVK