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Database: UniProt
Entry: K9P3M4_CYAGP
LinkDB: K9P3M4_CYAGP
Original site: K9P3M4_CYAGP 
ID   K9P3M4_CYAGP            Unreviewed;       220 AA.
AC   K9P3M4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Membrane-associated phospholipid phosphatase {ECO:0000313|EMBL:AFY27306.1};
GN   OrderedLocusNames=Cyagr_0086 {ECO:0000313|EMBL:AFY27306.1};
OS   Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Cyanobium.
OX   NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY27306.1, ECO:0000313|Proteomes:UP000010388};
RN   [1] {ECO:0000313|Proteomes:UP000010388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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DR   EMBL; CP003495; AFY27306.1; -; Genomic_DNA.
DR   RefSeq; WP_015107765.1; NC_019675.1.
DR   AlphaFoldDB; K9P3M4; -.
DR   STRING; 292564.Cyagr_0086; -.
DR   KEGG; cgc:Cyagr_0086; -.
DR   eggNOG; COG0671; Bacteria.
DR   HOGENOM; CLU_072573_3_0_3; -.
DR   OrthoDB; 9789113at2; -.
DR   Proteomes; UP000010388; Chromosome.
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; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR14969:SF13; AT30094P; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        62..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..198
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   220 AA;  23910 MW;  1538DDB016A2EC22 CRC64;
     MRFHLLPRER ILLPGCLIAL VGLFVAVAPG RPLALLDAAV LDWLGNHFHG LVGGVLTQVY
     RATGVGFTAV LVAMALVHLL RRRWWRDLRL LVMATGGILI LVDLVFKPLF SRQRPPGSLL
     PLDGHSFPSG HAAGAVAFYF AMVVILGSHH PRLRRTLALV ACALVGLVWL STLYVRAHWP
     TDLLAGAAVG LAWLTVCLAF WRDPPPVDPQ SGAARPLRSP
//
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