ID   DPRP_MYCS2              Reviewed;         180 AA.
AC   A0R627;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Putative decaprenylphosphoryl-5-phosphoribose phosphatase MSMEG_6402;
DE            Short=DPPR phosphatase;
DE            EC=3.1.3.-;
DE   AltName: Full=Phospholipid phosphatase;
GN   OrderedLocusNames=MSMEG_6402, MSMEI_6234;
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 DISRUPTION PHENOTYPE.
RX   PubMed=21575707; DOI=10.1016/j.micpath.2011.04.005;
RA   Jiang T., He L., Zhan Y., Zang S., Ma Y., Zhao X., Zhang C., Xin Y.;
RT   "The effect of MSMEG_6402 gene disruption on the cell wall structure of
RT   Mycobacterium smegmatis.";
RL   Microb. Pathog. 51:156-160(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). {ECO:0000269|PubMed:21575707}.
CC   -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Cells laking this gene show a reduced growth rate
CC       and deformation on the side. Cytoplasm is detached from the cell wall
CC       and possesses a discrepancy density compared to wild-type. The content
CC       of D-arabinofuran residues (Araf) is reduced significantly.
CC       {ECO:0000269|PubMed:21575707}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000480; ABK71187.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42660.1; -; Genomic_DNA.
DR   RefSeq; WP_003897811.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890615.1; NC_008596.1.
DR   AlphaFoldDB; A0R627; -.
DR   SMR; A0R627; -.
DR   STRING; 246196.MSMEI_6234; -.
DR   PRIDE; A0R627; -.
DR   EnsemblBacteria; ABK71187; ABK71187; MSMEG_6402.
DR   EnsemblBacteria; AFP42660; AFP42660; MSMEI_6234.
DR   GeneID; 66737679; -.
DR   KEGG; msg:MSMEI_6234; -.
DR   KEGG; msm:MSMEG_6402; -.
DR   PATRIC; fig|246196.19.peg.6228; -.
DR   eggNOG; COG0671; Bacteria.
DR   OMA; QWAGVAV; -.
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: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 wall biogenesis/degradation; Hydrolase; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..180
FT                   /note="Putative decaprenylphosphoryl-5-phosphoribose
FT                   phosphatase MSMEG_6402"
FT                   /id="PRO_0000420589"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   180 AA;  17975 MW;  AF178A3398A80EB8 CRC64;
     MSDAPRGEDA VLVAVQAALA GRPGVLTGAR ALSHFGEHSA GWVALAAAGA LAQPAKRRSW
     LAVGAGAFLA HAAAVVIKRV VRRERPSHPD IAVNVGTPSR LSFPSAHATS TTAAAVLLAQ
     TTGVPAPALL VPPMALSRLV LGVHYPTDVV TGVVVGALVG KAVGKAAGRI SNSVGAEGDR