ESTR_MYCTU
ID ESTR_MYCTU Reviewed; 456 AA.
AC P9WM39; L0T8Y0; Q10614;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Esterase Rv1288 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:30560095};
GN OrderedLocusNames=Rv1288; ORFNames=MTCY373.07;
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 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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, INDUCTION, DOMAIN, OVEREXPRESSION IN M.SMEGMATIS, MUTAGENESIS OF
RP SER-294; ASP-391 AND HIS-425, AND ACTIVE SITE.
RX PubMed=30560095; DOI=10.3389/fcimb.2018.00421;
RA Maan P., Kumar A., Kaur J., Kaur J.;
RT "Rv1288, a two domain, cell wall anchored, nutrient stress inducible
RT carboxyl-esterase of Mycobacterium tuberculosis, modulates cell wall
RT lipid.";
RL Front. Cell. Infect. Microbiol. 8:421-421(2018).
CC -!- FUNCTION: Exhibits lipolytic activity with medium chain length esters
CC as optimum substrates (PubMed:30560095). In vitro, pNP-caprylate (C8)
CC is the optimum substrate followed by pNP-capricate (C10)
CC (PubMed:30560095). May modulate the cell wall lipids to favor the
CC survival of bacteria under stress conditions (PubMed:30560095).
CC {ECO:0000269|PubMed:30560095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol
CC + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748;
CC Evidence={ECO:0000269|PubMed:30560095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC Evidence={ECO:0000269|PubMed:30560095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate +
CC H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658;
CC Evidence={ECO:0000269|PubMed:30560095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate
CC + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659;
CC Evidence={ECO:0000269|PubMed:30560095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:30560095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622;
CC Evidence={ECO:0000269|PubMed:30560095};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:30560095};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77 uM for pNP-caprylate {ECO:0000269|PubMed:30560095};
CC Note=kcat is 2 min(-1) with pNP-caprylate as substrate.
CC {ECO:0000269|PubMed:30560095};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:30560095};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:30560095};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:30560095}. Note=Cell wall anchored. Binds
CC peptidoglycans via the LytM domains. {ECO:0000269|PubMed:30560095}.
CC -!- INDUCTION: Expression is up-regulated under nutrient depletion
CC condition. {ECO:0000269|PubMed:30560095}.
CC -!- DOMAIN: Contains an N-terminal LytE region, which consists of three
CC consecutive LysM domains, and a C-terminal esterase domain. LytM
CC domains are essential for anchoring protein to the cell wall. The
CC presence of LytM domains results in enhanced rate of protein
CC aggregation at higher temperature. {ECO:0000269|PubMed:30560095}.
CC -!- MISCELLANEOUS: Overexpression in M.smegmatis leads to change in colony
CC morphology, enhanced pellicle and aggregate formation, which may be
CC linked with the changed lipid composition of the cell wall. Cell wall
CC has higher amount of lipids, with a significant increase in trehalose
CC dimycolate content. Overexpression also leads to increased drug
CC resistance and enhanced intracellular survival inside the macrophage
CC cell line. {ECO:0000269|PubMed:30560095}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44044.1; -; Genomic_DNA.
DR PIR; D70772; D70772.
DR RefSeq; NP_215804.1; NC_000962.3.
DR RefSeq; WP_003406625.1; NZ_NVQJ01000030.1.
DR AlphaFoldDB; P9WM39; -.
DR SMR; P9WM39; -.
DR STRING; 83332.Rv1288; -.
DR SwissLipids; SLP:000001945; -.
DR ESTHER; myctu-yc88; A85-Mycolyl-transferase.
DR PaxDb; P9WM39; -.
DR DNASU; 886974; -.
DR GeneID; 886974; -.
DR KEGG; mtu:Rv1288; -.
DR TubercuList; Rv1288; -.
DR eggNOG; COG0627; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR OMA; DPRMWYY; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071769; P:mycolate cell wall layer assembly; IBA:GO_Central.
DR CDD; cd00118; LysM; 3.
DR Gene3D; 3.10.350.10; -; 3.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR Pfam; PF00756; Esterase; 1.
DR Pfam; PF01476; LysM; 3.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 3.
PE 1: Evidence at protein level;
KW Cell wall; Hydrolase; Lipid metabolism; Reference proteome; Repeat;
KW Secreted; Serine esterase.
FT CHAIN 1..456
FT /note="Esterase Rv1288"
FT /id="PRO_0000103786"
FT DOMAIN 3..50
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 54..101
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 105..152
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT ACT_SITE 294
FT /evidence="ECO:0000305|PubMed:30560095"
FT ACT_SITE 391
FT /evidence="ECO:0000305|PubMed:30560095"
FT ACT_SITE 425
FT /evidence="ECO:0000305|PubMed:30560095"
FT MUTAGEN 294
FT /note="S->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:30560095"
FT MUTAGEN 391
FT /note="D->A: 85% reduction of activity."
FT /evidence="ECO:0000269|PubMed:30560095"
FT MUTAGEN 425
FT /note="H->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:30560095"
SQ SEQUENCE 456 AA; 49619 MW; 9B70C0471EDF113A CRC64;
MVSTHAVVAG ETLSALALRF YGDAELYRLI AAASGIADPD VVNVGQRLIM PDFTRYTVVA
GDTLSALALR FYGDAELNWL IAAASGIADP DVVNVGQRLI MPDFTRYTVV AGDTLSALAA
RFYGDASLYP LIAAVNGIAD PGVIDVGQVL VIFIGRSDGF GLRIVDRNEN DPRLWYYRFQ
TSAIGWNPGV NVLLPDDYRT SGRTYPVLYL FHGGGTDQDF RTFDFLGIRD LTAGKPIIIV
MPDGGHAGWY SNPVSSFVGP RNWETFHIAQ LLPWIEANFR TYAEYDGRAV AGFSMGGFGA
LKYAAKYYGH FASASSHSGP ASLRRDFGLV VHWANLSSAV LDLGGGTVYG APLWDQARVS
ADNPVERIDS YRNKRIFLVA GTSPDPANWF DSVNETQVLA GQREFRERLS NAGIPHESHE
VPGGHVFRPD MFRLDLDGIV ARLRPASIGA AAERAD
