PE_MYCS2
ID PE_MYCS2 Reviewed; 383 AA.
AC Q2M5K2; A0QPI7; I7FDB0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Acyltransferase PE {ECO:0000303|PubMed:27028886, ECO:0000303|PubMed:32554804};
DE EC=2.3.1.- {ECO:0000269|PubMed:27028886};
DE AltName: Full=Proline-glutamic acid-rich protein {ECO:0000303|PubMed:27028886};
DE Short=PE protein {ECO:0000303|PubMed:27028886};
DE Flags: Precursor;
GN Name=pE {ECO:0000312|EMBL:ABC70855.1, ECO:0000312|EMBL:AFP36883.1};
GN OrderedLocusNames=MSMEG_0412 {ECO:0000312|EMBL:ABK73879.1},
GN MSMEI_0402 {ECO:0000312|EMBL:AFP36883.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000312|EMBL:ABC70855.1};
RN [1] {ECO:0000312|EMBL:ABC70855.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|EMBL:ABC70855.1};
RA Deshayes C., Kocincova D., Etienne G., Reyrat J.-M.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:ABK73879.1, ECO:0000312|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|EMBL:ABK73879.1,
RC ECO:0000312|Proteomes:UP000000757};
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 [3] {ECO:0000312|EMBL:AFP36883.1, ECO:0000312|Proteomes:UP000006158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000006158};
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 [4] {ECO:0000312|EMBL:AFP36883.1, ECO:0000312|Proteomes:UP000006158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000312|Proteomes:UP000006158};
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 [5]
RP PROTEIN SEQUENCE OF 54-73; 74-84; 85-101; 102-211 AND 283-383, FUNCTION,
RP PATHWAY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, PTM,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 26-ALA--ASP-29.
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000303|PubMed:32554804};
RX PubMed=32554804; DOI=10.1074/jbc.ra120.013299;
RA Thouvenel L., Prevot G., Chiaradia L., Parra J., Mouton-Barbosa E.,
RA Locard-Paulet M., Marcoux J., Tropis M., Burlet-Schiltz O., Daffe M.,
RA Guilhot C., Etienne G., Chalut C.;
RT "The final assembly of trehalose polyphleates takes place within the outer
RT layer of the mycobacterial cell envelope.";
RL J. Biol. Chem. 295:11184-11194(2020).
RN [6]
RP SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP 1-MET--ALA-28, AND BIOTECHNOLOGY.
RX PubMed=27825305; DOI=10.1186/s12866-016-0888-z;
RA Zanfardino A., Migliardi A., D'Alonzo D., Lombardi A., Varcamonti M.,
RA Cordone A.;
RT "Inactivation of MSMEG_0412 gene drastically affects surface related
RT properties of Mycobacterium smegmatis.";
RL BMC Microbiol. 16:267-267(2016).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=27028886; DOI=10.1016/j.chembiol.2015.11.013;
RA Burbaud S., Laval F., Lemassu A., Daffe M., Guilhot C., Chalut C.;
RT "Trehalose Polyphleates Are Produced by a Glycolipid Biosynthetic Pathway
RT Conserved across Phylogenetically Distant Mycobacteria.";
RL Cell Chem. Biol. 23:278-289(2016).
CC -!- FUNCTION: Acyltransferase involved in the biosynthesis of trehalose
CC polyphleates (TPP) (PubMed:32554804, PubMed:27028886). Catalyzes the
CC transfer of phleic acids onto 2,3-diacyl trehalose (DAT) to form TPP,
CC high-molecular-weight surface-exposed glycolipids consisting of
CC octoacylated trehalose with seven C36:5 and C40:6 polyunsaturated fatty
CC acids (phleic acids) and a C14-C19 fatty acid residue
CC (PubMed:27028886). {ECO:0000269|PubMed:27028886,
CC ECO:0000269|PubMed:32554804}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000269|PubMed:27028886,
CC ECO:0000269|PubMed:32554804}.
CC -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000269|PubMed:32554804}.
CC Secreted, cell wall {ECO:0000269|PubMed:27825305,
CC ECO:0000269|PubMed:32554804}.
CC -!- INDUCTION: By lipidic substrates. Expression is induced approximately
CC 50-fold in the presence of Tween 80 and 2-fold in the presence of
CC tributyrin. {ECO:0000269|PubMed:27825305}.
CC -!- PTM: Proteolytic cleavage of the signal peptide is required for export
CC to the cell envelope and for production of trehalose polyphleates
CC (TPP). {ECO:0000269|PubMed:32554804}.
CC -!- DISRUPTION PHENOTYPE: Change in bacterial surface properties resulting
CC in lack of sliding motility, altered biofilm formation, rough colony
CC phenotype, slower growth rate and enhanced susceptibility to
CC antimicrobial drugs including rifampicin and erythromycin
CC (PubMed:27825305). Loss of trehalose polyphleates (TPP) production
CC (PubMed:32554804, PubMed:27028886). {ECO:0000269|PubMed:27028886,
CC ECO:0000269|PubMed:27825305, ECO:0000269|PubMed:32554804}.
CC -!- BIOTECHNOLOGY: Potential target to impair mycobacterial growth and to
CC increase drug susceptibility. {ECO:0000305|PubMed:27825305}.
CC -!- SIMILARITY: Belongs to the mycobacterial PPE family. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:27825305, lack of this gene leads to loss
CC of glycopeptidolipids (GPLs) of the cell wall, but according to
CC PubMed:27028886, this protein is not involved in the biosynthesis of
CC GPLs. {ECO:0000269|PubMed:27028886, ECO:0000269|PubMed:27825305}.
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DR EMBL; AY439015; ABC70855.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK73879.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36883.1; -; Genomic_DNA.
DR RefSeq; WP_011726926.1; NZ_SIJM01000040.1.
DR RefSeq; YP_884825.1; NC_008596.1.
DR AlphaFoldDB; Q2M5K2; -.
DR STRING; 246196.MSMEI_0402; -.
DR ESTHER; mycs2-q2m5k2; PE-PPE.
DR EnsemblBacteria; ABK73879; ABK73879; MSMEG_0412.
DR EnsemblBacteria; AFP36883; AFP36883; MSMEI_0402.
DR GeneID; 66738598; -.
DR KEGG; msg:MSMEI_0402; -.
DR KEGG; msm:MSMEG_0412; -.
DR PATRIC; fig|246196.19.peg.408; -.
DR eggNOG; COG5651; Bacteria.
DR OMA; MVPPQNI; -.
DR OrthoDB; 1079716at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0031975; C:envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR013228; PE-PPE_C.
DR Pfam; PF08237; PE-PPE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell wall; Direct protein sequencing; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..28
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32554804"
FT CHAIN 29..383
FT /note="Acyltransferase PE"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32554804"
FT /id="PRO_5010137016"
FT DOMAIN 80..325
FT /note="PE-PPE"
FT /evidence="ECO:0000255"
FT MUTAGEN 1..28
FT /note="Missing: Loss of export to the cell wall."
FT /evidence="ECO:0000269|PubMed:27825305"
FT MUTAGEN 26..29
FT /note="Missing: Defective in trehalose polyphleates (TPP)
FT production, accumulating diacyl trehalose (DAT) precursors
FT due to uncleaved signal sequence."
FT /evidence="ECO:0000269|PubMed:32554804"
SQ SEQUENCE 383 AA; 40192 MW; DD930167EFC1055F CRC64;
MRRRLLAFGT AFTTIGTAGF LGFGVAAADD TKPVDPAPGG AHAEAPSMGT PGRGYALGGA
HVLGIPYDEY IMRTGADWFP GLDRQIVDYP AGQVQGHTLE RLFPGIGALG ERFMPGLGLD
GPSYGESIDV GAPNLINAIR QGGPGTVIGL SEGASVLDEV QARLAYDPAA PPPDSLSFAT
YGNPVGKHAF GESFLTQMFP VGSVVPSLDY RIPAPVESQY DTYQFVSAYD SIADWPDRPD
NWISVANAIV GLATGHTAVA FTNPSMVPPQ NIRTTVNSRG AKDTTIMIPE EHLPLVLPFK
YLGVDKDTLN KLDGVLKPYV DAGYSRNDDP LTAPITVDPV NGYDPAAVTA PATQAAFGGG
TDPVSQLLAG LQYVVNNQPA PKP
