ID Q9RUM9_DEIRA Unreviewed; 260 AA.
AC Q9RUM9;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 08-NOV-2023, entry version 108.
DE SubName: Full=Phosphatidylglycerophosphatase B-related protein {ECO:0000313|EMBL:AAF10927.1};
GN OrderedLocusNames=DR_1355 {ECO:0000313|EMBL:AAF10927.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF10927.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF10927.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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DR EMBL; AE000513; AAF10927.1; -; Genomic_DNA.
DR PIR; D75404; D75404.
DR RefSeq; NP_295078.1; NC_001263.1.
DR RefSeq; WP_010887996.1; NZ_JMLF01000006.1.
DR AlphaFoldDB; Q9RUM9; -.
DR STRING; 243230.DR_1355; -.
DR PaxDb; 243230-DR_1355; -.
DR EnsemblBacteria; AAF10927; AAF10927; DR_1355.
DR GeneID; 69517600; -.
DR KEGG; dra:DR_1355; -.
DR PATRIC; fig|243230.17.peg.1552; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_072573_3_0_0; -.
DR InParanoid; Q9RUM9; -.
DR OMA; VIWLWCK; -.
DR OrthoDB; 9789113at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03392; PAP2_like_2; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 2.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR14969:SF54; PHOSPHATIDYLGLYCEROPHOSPHATASE B; 1.
DR PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..225
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 260 AA; 27928 MW; 47210873F17C3417 CRC64;
MPAAPTPPTS SPPNPVSPAP TPPPQHIIRQ HGRTVLLLLL AVLAPLLLFA DLADDVLKHG
GFVWDRTILE WYAARRTPGL TQAAQVLALV AGVGGLPIIT LLVAWGLHRA RANVHAAFLV
LAVAGATLLN VLAKVMFHRP RPDELIAVLR EPGFSFPSGH AMANAAFGIA LALAFWRSKA
GWPLVVFGVL WALLVGASRN YLGVHYPSDV LAGFLASTAW VFGLYLTMGQ RWPALRRAPA
GEHDTRPPLK RPAVRPADEK
//