DPRP_MYCTO
ID DPRP_MYCTO Reviewed; 177 AA.
AC P9WI52; F2GDG6; L0TGM5; O53584; Q7D4U5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Putative decaprenylphosphoryl-5-phosphoribose phosphatase MT3914;
DE Short=DPPR phosphatase;
DE EC=3.1.3.-;
DE AltName: Full=Phospholipid phosphatase;
GN OrderedLocusNames=MT3914;
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. Could be involved in the dephosphorylation of
CC decaprenylphosphoryl-5-phosphoribose (DPPR) to decaprenyl-phospho-
CC ribose (DPR) (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK48280.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WI53};
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DR EMBL; AE000516; AAK48280.1; ALT_INIT; Genomic_DNA.
DR PIR; C70888; C70888.
DR RefSeq; WP_003420792.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WI52; -.
DR SMR; P9WI52; -.
DR EnsemblBacteria; AAK48280; AAK48280; MT3914.
DR KEGG; mtc:MT3914; -.
DR PATRIC; fig|83331.31.peg.4211; -.
DR HOGENOM; CLU_072573_7_1_11; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..177
FT /note="Putative decaprenylphosphoryl-5-phosphoribose
FT phosphatase MT3914"
FT /id="PRO_0000428067"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 177 AA; 18486 MW; 8C6EDB9621E116EA CRC64;
MAERAPRGEV AVMVAVQSAL VDRPGMLATA RGLSHFGEHC IGWLILALLG AIALPRRRRE
WLVAGAGAFV AHAIAVLIKR LVRRQRPDHP AIAVNVDTPS QLSFPSAHAT STTAAALLMG
RATGLPLPVV LVPPMALSRI LLGVHYPSDV AVGVALGATV GAIVDSVGGG RQRARKR
