ID A0A0Q5PVG9_9FLAO Unreviewed; 199 AA.
AC A0A0Q5PVG9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Phosphatidic acid phosphatase {ECO:0000313|EMBL:KQR90876.1};
GN ORFNames=ASG01_15045 {ECO:0000313|EMBL:KQR90876.1};
OS Chryseobacterium sp. Leaf180.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1736289 {ECO:0000313|EMBL:KQR90876.1, ECO:0000313|Proteomes:UP000051405};
RN [1] {ECO:0000313|EMBL:KQR90876.1, ECO:0000313|Proteomes:UP000051405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf180 {ECO:0000313|EMBL:KQR90876.1,
RC ECO:0000313|Proteomes:UP000051405};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf180 {ECO:0000313|Proteomes:UP000051405};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQR90876.1}.
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DR EMBL; LMPJ01000014; KQR90876.1; -; Genomic_DNA.
DR RefSeq; WP_055865781.1; NZ_LMPJ01000014.1.
DR AlphaFoldDB; A0A0Q5PVG9; -.
DR STRING; 1736289.ASG01_15045; -.
DR OrthoDB; 9789113at2; -.
DR Proteomes; UP000051405; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03395; PAP2_like_4; 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 Reference proteome {ECO:0000313|Proteomes:UP000051405};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..180
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 199 AA; 22700 MW; 3A4FB04F7343267A CRC64;
MNSTLDHLKA FDTELFLMIN RQHNAFFDIV MYWASDKLFW FPFYAVLLFF LISIYKKFTI
FILLAITATI TLCDQTASGL LKNLVKRLRP SHEPDLAPFV HLSKAGAGGN YGFVSSHSAN
AFGLVIFLFF LLPAKYNWLK IILLFWALLV SYSRIYNGVH YPGDIIGGAF VGCISGSVVW
LIFRRIFRNS KVGERHLST
//
