PPM1_MYCS2
ID PPM1_MYCS2 Reviewed; 265 AA.
AC A0QZ12;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Polyprenol monophosphomannose synthase;
DE Short=PPM synthase;
DE Short=Polyprenol-P-Man synthase {ECO:0000303|PubMed:12427759};
DE Short=Ppm1 {ECO:0000303|PubMed:12427759};
DE EC=2.4.1.- {ECO:0000269|PubMed:23118955};
DE AltName: Full=Dolichol-phosphate mannose synthase {ECO:0000303|PubMed:12427759};
DE EC=2.4.1.83 {ECO:0000269|PubMed:12427759};
GN Name=ppm1 {ECO:0000303|PubMed:12427759};
GN OrderedLocusNames=MSMEG_3859, MSMEI_3769;
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, SUBUNIT, SUBCELLULAR LOCATION, AND EXPRESSION
RP IN E.COLI.
RX PubMed=12427759; DOI=10.1074/jbc.m207922200;
RA Baulard A.R., Gurcha S.S., Engohang-Ndong J., Gouffi K., Locht C.,
RA Besra G.S.;
RT "In vivo interaction between the polyprenol phosphate mannose synthase Ppm1
RT and the integral membrane protein Ppm2 from Mycobacterium smegmatis
RT revealed by a bacterial two-hybrid system.";
RL J. Biol. Chem. 278:2242-2248(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=23118955; DOI=10.1371/journal.pone.0048211;
RA Rana A.K., Singh A., Gurcha S.S., Cox L.R., Bhatt A., Besra G.S.;
RT "Ppm1-encoded polyprenyl monophosphomannose synthase activity is essential
RT for lipoglycan synthesis and survival in mycobacteria.";
RL PLoS ONE 7:E48211-E48211(2012).
CC -!- FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors to form
CC polyprenol monophosphomannose (PPM); catalytic activity in vitro is
CC enhanced by Lnt (AC A0QZ13) (PubMed:12427759). PMM is an alkai-stable
CC sugar donor which adds mannose-phosphate residues to triacylated-PIM2,
CC eventually leading to generation of the cell wall glycolipid lipoglycan
CC modulins lipoarabinomannan (LAM) and lipomannan (LM) (By similarity).
CC {ECO:0000250|UniProtKB:O53493, ECO:0000269|PubMed:12427759,
CC ECO:0000269|PubMed:23118955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-
CC D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83;
CC Evidence={ECO:0000269|PubMed:12427759};
CC -!- SUBUNIT: Interacts with Lnt (also called Ppm2, AC A0QZ13) upon
CC coexpression in E.coli, which increases the PPM synthase activity of
CC this protein. {ECO:0000269|PubMed:12427759}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12427759}.
CC -!- DISRUPTION PHENOTYPE: Essential it cannot be deleted. In depletion
CC experiments increasing amounts of phosphatidyl-myo-inositol (PI) and
CC decreasing amounts of acylated PI mannosides (AcPIM), as well as
CC decreased synthesis of lipomannan (LM) but not lipoarabinomannan (LAM)
CC are observed. {ECO:0000269|PubMed:23118955}.
CC -!- MISCELLANEOUS: In a number of other Mycobacteria, including M.bovis and
CC M.tuberculosis, this protein is the first domain in a 2 domain protein.
CC {ECO:0000305|PubMed:12427759}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; CP000480; ABK72511.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40227.1; -; Genomic_DNA.
DR RefSeq; WP_003895306.1; NZ_SIJM01000005.1.
DR RefSeq; YP_888150.1; NC_008596.1.
DR AlphaFoldDB; A0QZ12; -.
DR SMR; A0QZ12; -.
DR STRING; 246196.MSMEI_3769; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; A0QZ12; -.
DR EnsemblBacteria; ABK72511; ABK72511; MSMEG_3859.
DR EnsemblBacteria; AFP40227; AFP40227; MSMEI_3769.
DR GeneID; 66735226; -.
DR KEGG; msg:MSMEI_3769; -.
DR KEGG; msm:MSMEG_3859; -.
DR PATRIC; fig|246196.19.peg.3798; -.
DR eggNOG; COG0463; Bacteria.
DR OMA; TAYIHGF; -.
DR OrthoDB; 1064289at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd06442; DPM1_like; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398; PTHR43398; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..265
FT /note="Polyprenol monophosphomannose synthase"
FT /id="PRO_0000434584"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 29106 MW; 66EEF42D84C6B572 CRC64;
MSVPGEREQG AGEDPATVRP TQRTLVIIPT YNERENLPLI VGRVHHACPQ VHILVVDDGS
PDGTGALADE LALADPDRVH VMHRTSKAGL GAAYLAGFDW GLRRGYSVLV EMDADGSHAP
EELSRLLDAV DAGADLAIGS RYVPGGTVRN WPWRRLVLSK TANTYSRFLL GVGIHDITAG
YRAYRREVLE KIDLSAVDSK GYCFQIDLTW RAINNGFSVV EVPITFTERE LGVSKMSGSN
IREAMFKVAE WGIRGRLDRA RGVVR
