ID A0A1B8J6R0_9HELI Unreviewed; 270 AA.
AC A0A1B8J6R0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN ORFNames=BA723_01635 {ECO:0000313|EMBL:OBV28599.1}, BKN38_07030
GN {ECO:0000313|EMBL:OHU82520.1};
OS Helicobacter sp. CLO-3.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=211 {ECO:0000313|EMBL:OBV28599.1, ECO:0000313|Proteomes:UP000092701};
RN [1] {ECO:0000313|EMBL:OBV28599.1, ECO:0000313|Proteomes:UP000092701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC1 {ECO:0000313|EMBL:OBV28599.1,
RC ECO:0000313|Proteomes:UP000092701};
RA Greninger A.L., Bateman A., Jerome K., Fang F.;
RT "Genome sequence of Helicobacter sp. CLO-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OHU82520.1, ECO:0000313|Proteomes:UP000179541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLO-3 {ECO:0000313|EMBL:OHU82520.1,
RC ECO:0000313|Proteomes:UP000179541};
RA Greninger A.L., Bateman A.C., Fang F., Jerome K.;
RT "Genome sequence of Helicobacter sp. CLO-3 Fennel-37 strain.";
RL Submitted (OCT-2016) 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:OBV28599.1}.
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DR EMBL; MAMQ01000105; OBV28599.1; -; Genomic_DNA.
DR EMBL; MLQN01000023; OHU82520.1; -; Genomic_DNA.
DR RefSeq; WP_066457717.1; NZ_MLQN01000023.1.
DR AlphaFoldDB; A0A1B8J6R0; -.
DR STRING; 211.BKN38_07030; -.
DR Proteomes; UP000092701; Unassembled WGS sequence.
DR Proteomes; UP000179541; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR PANTHER; PTHR14969:SF60; UNDECAPRENYL-DIPHOSPHATASE YBJG-RELATED; 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:UP000092701};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..270
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008610684"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..232
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 46..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 28751 MW; 779069AE63E737D1 CRC64;
MYKKCGYLII ALGLCFGALN VANAESSDKA ASDKIAGDTA NSARAESALE SRLDSGADSS
KDSTKVDSAK SLESSNAIDS SKNADKYGDA FETFGDMAQF LPAASLGYAL LLRDFVGAKQ
QVIGFVAVVA TTHLIKYSLH FYTLHFSADD SKIAQLSKRP TRESYEAFPS GHTAASFSAV
GFLQKRYGAR LGIPAALIAS AVGISRVHSE NHTIVQVICG AMLGFFLSFL LTRARNPHDK
THPAKPELKG QAPSTKTMLC EISLLALAFL
//