DPPRS_MYCS2
ID DPPRS_MYCS2 Reviewed; 318 AA.
AC A0R626; I7GGE4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Decaprenyl-phosphate phosphoribosyltransferase;
DE EC=2.4.2.45;
DE AltName: Full=5-phospho-alpha-D-ribose-1-diphosphate:decaprenyl-phosphate 5-phosphoribosyltransferase;
DE AltName: Full=DPPR synthase;
GN OrderedLocusNames=MSMEG_6401, MSMEI_6233;
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, AND SUBCELLULAR LOCATION.
RX PubMed=18310020; DOI=10.1099/mic.0.2007/013532-0;
RA Huang H., Berg S., Spencer J.S., Vereecke D., D'Haeze W., Holsters M.,
RA McNeil M.R.;
RT "Identification of amino acids and domains required for catalytic activity
RT of DPPR synthase, a cell wall biosynthetic enzyme of Mycobacterium
RT tuberculosis.";
RL Microbiology 154:736-743(2008).
CC -!- FUNCTION: Involved in the biosynthesis of decaprenylphosphoryl
CC arabinose (DPA) a precursor for arabinan synthesis in mycobacterial
CC cell wall biosynthesis. Catalyzes the transfer of a 5-phosphoribosyl
CC residue from phosphoribose diphosphate (pRpp) to decaprenyl phosphate
CC (DP) to form decaprenylphosphoryl-5-phosphoribose (DPPR).
CC {ECO:0000269|PubMed:18310020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + H(+) + trans,octa-
CC cis-decaprenyl phosphate = diphosphate + trans,octa-cis-
CC decaprenylphospho-beta-D-ribofuranose 5-phosphate;
CC Xref=Rhea:RHEA:34067, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:65079, ChEBI:CHEBI:66937; EC=2.4.2.45;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Divalent metal cations such as Mg(2+), Mn(2+) or Ca(2+).
CC {ECO:0000250};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:18310020}; Multi-
CC pass membrane protein {ECO:0000305|PubMed:18310020}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP42659.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK74962.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42659.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_890614.1; NC_008596.1.
DR AlphaFoldDB; A0R626; -.
DR SMR; A0R626; -.
DR STRING; 246196.MSMEI_6233; -.
DR PRIDE; A0R626; -.
DR EnsemblBacteria; ABK74962; ABK74962; MSMEG_6401.
DR EnsemblBacteria; AFP42659; AFP42659; MSMEI_6233.
DR KEGG; msg:MSMEI_6233; -.
DR KEGG; msm:MSMEG_6401; -.
DR PATRIC; fig|246196.19.peg.6227; -.
DR eggNOG; COG0382; Bacteria.
DR OMA; RWFLITT; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="Decaprenyl-phosphate phosphoribosyltransferase"
FT /id="PRO_0000420588"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 318 AA; 34527 MW; ACEA9944E050437A CRC64;
MDATHMSEEA QPTAGPPKNL VSGLIKAVRP RQWIKNLLVL AAPLAAVGSG IEYDYADVAA
KVSVAFVVFC LAASSIYLIN DARDVEADRA HPTKRFRPIA AGVVPEWMAY SLAGLLAVAS
LVISWWLTAN LAIVMAVYIA VQLAYCFGLK HQAVLDICIV SSGFLIRAIA GGVAADIPLS
QWFLLVMAFG SLFMAAGKRY AELQLAERTG AKIRKSLESY TSSYLRFVWT LSATAMVVCY
GLWAFSRDRA NDLMTLDAQD ASWYAVTMIP FTIAILRYAV DIDGGIAGEP EEIALKDRVL
QILFLAWIGT IGAAIYFS
