LIPR_MYCTU
ID LIPR_MYCTU Reviewed; 308 AA.
AC P9WK85; 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 40.
DE RecName: Full=Putative acetyl-hydrolase LipR;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=lipR; Synonyms=bah; OrderedLocusNames=Rv3084;
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 INDUCTION, AND GENE NAME.
RX PubMed=14568148; DOI=10.1016/s0378-1097(03)00648-7;
RA Singh A., Jain S., Gupta S., Das T., Tyagi A.K.;
RT "mymA operon of Mycobacterium tuberculosis: its regulation and importance
RT in the cell envelope.";
RL FEMS Microbiol. Lett. 227:53-63(2003).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Erdman;
RX PubMed=15937179; DOI=10.1128/jb.187.12.4173-4186.2005;
RA Singh A., Gupta R., Vishwakarma R.A., Narayanan P.R., Paramasivan C.N.,
RA Ramanathan V.D., Tyagi A.K.;
RT "Requirement of the mymA operon for appropriate cell wall ultrastructure
RT and persistence of Mycobacterium tuberculosis in the spleens of guinea
RT pigs.";
RL J. Bacteriol. 187:4173-4186(2005).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16893682; DOI=10.1016/j.tube.2006.01.021;
RA Cheruvu M., Plikaytis B.B., Shinnick T.M.;
RT "The acid-induced operon Rv3083-Rv3089 is required for growth of
RT Mycobacterium tuberculosis in macrophages.";
RL Tuberculosis 87:12-20(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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).
CC -!- FUNCTION: Required for maintaining the appropriate mycolic acid
CC composition and permeability of the envelope on its exposure to acidic
CC pH. {ECO:0000269|PubMed:15937179}.
CC -!- INDUCTION: Expression is controlled by VirS. Induced at acidic pH and
CC in macrophages. {ECO:0000269|PubMed:14568148}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the mymA operon causes altered
CC cell wall structure, reduced contents and altered composition of
CC mycolic acids along with the accumulation of saturated C24 and C26
CC fatty acids, and enhanced susceptibility to antibiotics, detergents and
CC acidic pH. Also impairs ability to survive in macrophages.
CC {ECO:0000269|PubMed:15937179, ECO:0000269|PubMed:16893682}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45893.1; -; Genomic_DNA.
DR PIR; H70852; H70852.
DR RefSeq; NP_217600.1; NC_000962.3.
DR RefSeq; WP_003901538.1; NZ_NVQJ01000011.1.
DR AlphaFoldDB; P9WK85; -.
DR SMR; P9WK85; -.
DR STRING; 83332.Rv3084; -.
DR ChEMBL; CHEMBL4105823; -.
DR ESTHER; myctu-Rv3084; Hormone-sensitive_lipase_like.
DR PaxDb; P9WK85; -.
DR DNASU; 888652; -.
DR GeneID; 888652; -.
DR KEGG; mtu:Rv3084; -.
DR TubercuList; Rv3084; -.
DR eggNOG; COG0657; Bacteria.
DR OMA; DVPHVFQ; -.
DR PhylomeDB; P9WK85; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0034338; F:short-chain carboxylesterase 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 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; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..308
FT /note="Putative acetyl-hydrolase LipR"
FT /id="PRO_0000420877"
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:O06350"
FT ACT_SITE 239
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 269
FT /evidence="ECO:0000250|UniProtKB:O06350"
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
