MGLL_MYCS2
ID MGLL_MYCS2 Reviewed; 280 AA.
AC A0QNZ7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Monoacylglycerol lipase {ECO:0000303|PubMed:20601476};
DE Short=MGL {ECO:0000303|PubMed:20601476};
DE EC=3.1.1.23 {ECO:0000269|PubMed:20601476};
GN OrderedLocusNames=MSMEG_0220, MSMEI_0213;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, MUTAGENESIS OF SER-111, SUBCELLULAR LOCATION, ACTIVE SITE, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=20601476; DOI=10.1128/jb.00261-10;
RA Dhouib R., Laval F., Carriere F., Daffe M., Canaan S.;
RT "A monoacylglycerol lipase from Mycobacterium smegmatis involved in
RT bacterial cell interaction.";
RL J. Bacteriol. 192:4776-4785(2010).
CC -!- FUNCTION: Contributes to cell growth, probably by hydrolyzing exogenous
CC lipids. Catalyzes the hydrolysis of monoacylglycerols (MAG) with fatty
CC acid chains ranging from C14 to C18, with a maximum activity on
CC monoolein. Is unable to hydrolyze long-chain diacylglycerol (DAG).
CC {ECO:0000269|PubMed:20601476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:20601476};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. Highly stable from pH 6.5 to 9.0, and still shows a
CC residual activity of 50% after 1 hour of incubation at pH 4.0.
CC {ECO:0000269|PubMed:20601476};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:20601476}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene affects the morphology of
CC the colony and impairs growth in the presence of monoolein. Cells
CC lacking this gene are more sensitive to rifampicin and more resistant
CC to isoniazid. {ECO:0000269|PubMed:20601476}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK74423.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36694.1; -; Genomic_DNA.
DR RefSeq; WP_011726751.1; NZ_SIJM01000047.1.
DR RefSeq; YP_884635.1; NC_008596.1.
DR AlphaFoldDB; A0QNZ7; -.
DR SMR; A0QNZ7; -.
DR STRING; 246196.MSMEI_0213; -.
DR ESTHER; mycs2-a0qnz7; Monoglyceridelipase_lysophospholip.
DR PRIDE; A0QNZ7; -.
DR EnsemblBacteria; ABK74423; ABK74423; MSMEG_0220.
DR EnsemblBacteria; AFP36694; AFP36694; MSMEI_0213.
DR GeneID; 66738408; -.
DR KEGG; msg:MSMEI_0213; -.
DR KEGG; msm:MSMEG_0220; -.
DR PATRIC; fig|246196.19.peg.216; -.
DR eggNOG; COG2267; Bacteria.
DR OMA; FHGFSDH; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cell wall; Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW Lipid biosynthesis; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted.
FT CHAIN 1..280
FT /note="Monoacylglycerol lipase"
FT /id="PRO_0000438238"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:20601476"
FT ACT_SITE 227
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O07427"
FT ACT_SITE 257
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O07427"
FT MUTAGEN 111
FT /note="S->A: Loss of lipase activity."
FT /evidence="ECO:0000269|PubMed:20601476"
SQ SEQUENCE 280 AA; 29882 MW; B64EC1DB638D80BF CRC64;
MVSSTRSEHS FAGVGGVRIV YDVWTPDTDP RGVVVLAHGY AEHAGRYHHV AQRFGAAGLL
VYALDHRGHG RSGGKRVHLR DLSEFVEDFR TLVGIAANDH PTLPRIVLGH SMGGGIVFAY
GARYPGEYSA MVLSGPAVNA HDGVSPVLVA VAKVLGKLAP GIPVENLDAD AVSRDPEVVA
AYKADPMVHH GKLPAGIARA LIGLGQSMPQ RAAALTAPLL VVHGDKDRLI PVAGSRLLVD
RVASEDVHLK VYPGLYHEVF NEPEQKLVLD DVTSWIVSHL
