DPPRS_MYCTO
ID DPPRS_MYCTO Reviewed; 302 AA.
AC P9WFR4; F2GDG5; L0TGT7; O53583; Q7D4U6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
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=MT3913;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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) (By
CC similarity). {ECO:0000250}.
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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK48279.1; -; Genomic_DNA.
DR PIR; B70888; B70888.
DR RefSeq; WP_003899704.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WFR4; -.
DR EnsemblBacteria; AAK48279; AAK48279; MT3913.
DR KEGG; mtc:MT3913; -.
DR PATRIC; fig|83331.31.peg.4210; -.
DR HOGENOM; CLU_029423_0_0_11; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001020; 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; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..302
FT /note="Decaprenyl-phosphate phosphoribosyltransferase"
FT /id="PRO_0000428491"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..54
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..169
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 265..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 302 AA; 32654 MW; B232C90EE4D32717 CRC64;
MSEDVVTQPP ANLVAGVVKA IRPRQWVKNV LVLAAPLAAL GGGVRYDYVE VLSKVSMAFV
VFSLAASAVY LVNDVRDVEA DREHPTKRFR PIAAGVVPEW LAYTVAVVLG VTSLAGAWML
TPNLALVMVV YLAMQLAYCF GLKHQAVVEI CVVSSAYLIR AIAGGVATKI PLSKWFLLIM
AFGSLFMVAG KRYAELHLAE RTGAAIRKSL ESYTSTYLRF VWTLSATAVV LCYGLWAFER
DGYSGSWFAV SMIPFTIAIL RYAVDVDGGL AGEPEDIALR DRVLQLLALA WIATVGAAVA
FG
