PE11_MYCTU
ID PE11_MYCTU Reviewed; 100 AA.
AC Q79FR5; I6XX98; L0T7I0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Esterase PE11 {ECO:0000305};
DE EC=3.1.1.6 {ECO:0000269|PubMed:26902658};
DE AltName: Full=PE family protein PE11 {ECO:0000305};
GN Name=PE11 {ECO:0000303|PubMed:23469198};
GN Synonyms=lipX {ECO:0000303|PubMed:16354661};
GN OrderedLocusNames=Rv1169c {ECO:0000312|EMBL:CCP43925.1};
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.
RX PubMed=16354661; DOI=10.1074/jbc.m505556200;
RA Deb C., Daniel J., Sirakova T.D., Abomoelak B., Dubey V.S.,
RA Kolattukudy P.E.;
RT "A novel lipase belonging to the hormone-sensitive lipase family induced
RT under starvation to utilize stored triacylglycerol in Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 281:3866-3875(2006).
RN [3]
RP INVOLVEMENT IN B-CELL RESPONSE.
RX PubMed=17687113; DOI=10.1128/cvi.00181-07;
RA Narayana Y., Joshi B., Katoch V.M., Mishra K.C., Balaji K.N.;
RT "Differential B-cell responses are induced by Mycobacterium tuberculosis PE
RT antigens Rv1169c, Rv0978c, and Rv1818c.";
RL Clin. Vaccine Immunol. 14:1334-1341(2007).
RN [4]
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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=23469198; DOI=10.1371/journal.pone.0057517;
RA Dona V., Ventura M., Sali M., Cascioferro A., Provvedi R., Palu G.,
RA Delogu G., Manganelli R.;
RT "The PPE domain of PPE17 is responsible for its surface localization and
RT can be used to express heterologous proteins on the mycobacterial
RT surface.";
RL PLoS ONE 8:e57517-e57517(2013).
RN [6]
RP FUNCTION, EXPRESSION IN M.SMEGMATIS, AND SUBCELLULAR LOCATION.
RX PubMed=26157429; DOI=10.3389/fmicb.2015.00613;
RA Deng W., Zeng J., Xiang X., Li P., Xie J.;
RT "PE11 (Rv1169c) selectively alters fatty acid components of Mycobacterium
RT smegmatis and host cell interleukin-6 level accompanied with cell death.";
RL Front. Microbiol. 6:613-613(2015).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND EXPRESSION IN M.SMEGMATIS.
RX PubMed=26902658; DOI=10.1038/srep21624;
RA Singh P., Rao R.N., Reddy J.R., Prasad R.B., Kotturu S.K., Ghosh S.,
RA Mukhopadhyay S.;
RT "PE11, a PE/PPE family protein of Mycobacterium tuberculosis is involved in
RT cell wall remodeling and virulence.";
RL Sci. Rep. 6:21624-21624(2016).
RN [8]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28198348; DOI=10.1099/mic.0.000417;
RA Rastogi S., Singh A.K., Pant G., Mitra K., Sashidhara K.V., Krishnan M.Y.;
RT "Down-regulation of PE11, a cell wall associated esterase, enhances the
RT biofilm growth of Mycobacterium tuberculosis and reduces cell wall
RT virulence lipid levels.";
RL Microbiology 163:52-61(2017).
CC -!- FUNCTION: Involved in cell wall lipids remodeling and in virulence
CC (PubMed:26157429, PubMed:26902658, PubMed:28198348). Restricts the
CC biofilm growth and is essential for the optimal intracellular survival
CC of M.tuberculosis (PubMed:28198348). Shows esterase activity with a
CC preference for short-chain esters, particularly pNP-acetate (C2) and
CC pNP-butyrate (C4) (PubMed:26902658). Has weaker activity with pNP-
CC octanoate (C8), pNP-laurate (C12) and pNP-myristate (C14)
CC (PubMed:26902658). Shows weak long-chain triacylglycerol (TAG)
CC hydrolase activity in vitro (PubMed:16354661). Not necessary for PPE17
CC stability or for its localization on the mycobacterial surface
CC (PubMed:23469198). {ECO:0000269|PubMed:16354661,
CC ECO:0000269|PubMed:23469198, ECO:0000269|PubMed:26157429,
CC ECO:0000269|PubMed:26902658, ECO:0000269|PubMed:28198348}.
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; EC=3.1.1.6;
CC Evidence={ECO:0000269|PubMed:26902658};
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:26902658};
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:26902658};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:26157429}. Note=Cell wall associated protein.
CC {ECO:0000269|PubMed:26157429}.
CC -!- INDUCTION: Coexpressed with PPE17. {ECO:0000269|PubMed:23469198,
CC ECO:0000269|PubMed:28198348}.
CC -!- DISRUPTION PHENOTYPE: Knock-down of the gene alters the colony
CC morphology and slows down growth. Knock-down induces aggregation, early
CC biofilm formation and changes in cell wall lipid composition. It also
CC results in decreased survival of Mycobacterium inside macrophages and
CC reduced necrotic death of THP-1 macrophages.
CC {ECO:0000269|PubMed:28198348}.
CC -!- MISCELLANEOUS: Elicits a strong B-cell humoral response among different
CC clinical categories of both adult and child tuberculosis patients.
CC {ECO:0000269|PubMed:17687113}.
CC -!- MISCELLANEOUS: Expression in non-pathogenic M.smegmatis (Msmeg) strain
CC induces necrotic cell death of macrophage after infection and
CC significantly decreased IL-6 production compared to controls
CC (PubMed:26157429). Msmeg-PE11 bacilli exhibit altered colony morphology
CC and cell wall lipid composition leading to a marked increase in
CC resistance against various environmental stressors and antibiotics
CC (PubMed:26902658). Mice infected with Msmeg-PE11 have higher bacterial
CC load, show exacerbated organ pathology and mortality. The liver and
CC lung of Msmeg-PE11-infected mice have higher levels of IL-10, IL-4 and
CC TNF-alpha cytokines (PubMed:26902658). {ECO:0000269|PubMed:26157429,
CC ECO:0000269|PubMed:26902658}.
CC -!- SIMILARITY: Belongs to the mycobacterial PE family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43925.1; -; Genomic_DNA.
DR RefSeq; WP_003898752.1; NZ_NVQJ01000025.1.
DR RefSeq; YP_177792.1; NC_000962.3.
DR AlphaFoldDB; Q79FR5; -.
DR SMR; Q79FR5; -.
DR STRING; 83332.Rv1169c; -.
DR PaxDb; Q79FR5; -.
DR GeneID; 45425141; -.
DR GeneID; 885930; -.
DR KEGG; mtu:Rv1169c; -.
DR PATRIC; fig|83332.111.peg.1310; -.
DR TubercuList; Rv1169c; -.
DR OMA; CFVTTRP; -.
DR PhylomeDB; Q79FR5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008126; F:acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:MTBBASE.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR InterPro; IPR000084; PE-PGRS_N.
DR Pfam; PF00934; PE; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Hydrolase; Reference proteome;
KW Secreted; Virulence.
FT CHAIN 1..100
FT /note="Esterase PE11"
FT /id="PRO_0000451088"
FT DOMAIN 4..94
FT /note="PE"
FT /evidence="ECO:0000255"
SQ SEQUENCE 100 AA; 10872 MW; 82F436818463A897 CRC64;
MSFVTTRPDS IGETAANLHE IGVTMSAHDD GVTPLITNVE SPAHDLVSIV TSMLFSMHGE
LYKAIARQAH VIHESFVQTL QTSKTSYWLT ELANRAGTST
