ID A0A172YFM7_9GAMM Unreviewed; 470 AA.
AC A0A172YFM7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN ORFNames=A5892_10685 {ECO:0000313|EMBL:ANF57872.1};
OS Halotalea alkalilenta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halotalea.
OX NCBI_TaxID=376489 {ECO:0000313|EMBL:ANF57872.1, ECO:0000313|Proteomes:UP000077875};
RN [1] {ECO:0000313|EMBL:ANF57872.1, ECO:0000313|Proteomes:UP000077875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHB B 13600 {ECO:0000313|EMBL:ANF57872.1,
RC ECO:0000313|Proteomes:UP000077875};
RA Swarnkar M.K., Sharma A., Kaushal K., Soni R., Rana S., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequence of Halotalea alkalilenta IHB B 13600.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DedA family.
CC {ECO:0000256|ARBA:ARBA00010792}.
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DR EMBL; CP015243; ANF57872.1; -; Genomic_DNA.
DR RefSeq; WP_064122793.1; NZ_CP015243.1.
DR AlphaFoldDB; A0A172YFM7; -.
DR STRING; 376489.A5892_10685; -.
DR KEGG; haa:A5892_10685; -.
DR Proteomes; UP000077875; Chromosome.
DR GO; GO:0005886; C:plasma 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; IPR032818; DedA.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR032816; VTT_dom.
DR PANTHER; PTHR30353; INNER MEMBRANE PROTEIN DEDA-RELATED; 1.
DR PANTHER; PTHR30353:SF15; INNER MEMBRANE PROTEIN YABI; 1.
DR Pfam; PF01569; PAP2; 1.
DR Pfam; PF09335; SNARE_assoc; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077875};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 322..433
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 470 AA; 52585 MW; CD78AD1372C9DE64 CRC64;
MNLVAWVEPL TQTPWALLLL IGILAALESL AIIGLILPGA VMMTMAASLA GSVQLSVPLV
LLSGALGATI GDGLSYWLGA SQRHRIPKLW PLNRHPEWLE RGQLFFHRYG TLSVLLGRFV
GPVRPIIPMV AGMMCMPRRR FALVNALSAL GWAPLYILPG YYLGQAWSAN LALSHDTMVW
LIEFAFVTLL AILTFSWLRR LFDRPGIGYR SALGWARQSN AGRRLWRRLN GRFPGREPPL
ASLALLLATG FLFIVWTGVV LLHGREPLVM DLRGQAMFIE LAKLGWPLSI ASHFDLIGDT
YGIAAFTLPW LVWWLYRRYY AVLLHWMLAL GLISLLNTVL KQVIQRVRPD TPDHLANSFS
YPSAHTSAAV VVYGLAAAFV AQRLPRSQRS WPYWAATLLI MLMAISRLAY GVHWASDLIG
GALVGLMVCS TVRISYQYHA QQRLSWQHWP WVLGLSIVLL LARMLFLPQA
//
