ID   DPRP_MYCTU              Reviewed;         177 AA.
AC   P9WI53; 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 36.
DE   RecName: Full=Putative decaprenylphosphoryl-5-phosphoribose phosphatase Rv3807c;
DE            Short=DPPR phosphatase;
DE            EC=3.1.3.-;
DE   AltName: Full=Phospholipid phosphatase;
GN   OrderedLocusNames=Rv3807c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 8-31, AND SEQUENCE REVISION TO N-TERMINUS.
RC   STRAIN=H37Rv;
RX   PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA   Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA   Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT   "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT   annotated encoding genes.";
RL   Genomics 114:292-304(2022).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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=CCP46636.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR   EMBL; AL123456; CCP46636.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70888; C70888.
DR   RefSeq; NP_218324.1; NC_000962.3.
DR   RefSeq; WP_003420792.1; NC_000962.3.
DR   AlphaFoldDB; P9WI53; -.
DR   SMR; P9WI53; -.
DR   STRING; 83332.Rv3807c; -.
DR   PaxDb; P9WI53; -.
DR   DNASU; 886134; -.
DR   GeneID; 886134; -.
DR   KEGG; mtu:Rv3807c; -.
DR   PATRIC; fig|83332.111.peg.4232; -.
DR   TubercuList; Rv3807c; -.
DR   eggNOG; COG0671; Bacteria.
DR   OMA; QWAGVAV; -.
DR   PhylomeDB; P9WI53; -.
DR   BioCyc; MetaCyc:G185E-8103-MON; -.
DR   UniPathway; UPA00963; -.
DR   Proteomes; UP000001584; 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:0042392; F:sphingosine-1-phosphate phosphatase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cell membrane; Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Hydrolase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..177
FT                   /note="Putative decaprenylphosphoryl-5-phosphoribose
FT                   phosphatase Rv3807c"
FT                   /id="PRO_0000420590"
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