ID W4SNK5_9XANT Unreviewed; 702 AA.
AC W4SNK5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Membrane-associated phospholipid phosphatase {ECO:0000313|EMBL:GAE57907.1};
GN ORFNames=XPR_4542 {ECO:0000313|EMBL:GAE57907.1};
OS Xanthomonas arboricola pv. pruni MAFF 301420.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1418095 {ECO:0000313|EMBL:GAE57907.1, ECO:0000313|Proteomes:UP000019084};
RN [1] {ECO:0000313|EMBL:GAE57907.1, ECO:0000313|Proteomes:UP000019084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 301420 {ECO:0000313|Proteomes:UP000019084};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) 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}.
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:GAE57907.1}.
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DR EMBL; BAVC01000387; GAE57907.1; -; Genomic_DNA.
DR AlphaFoldDB; W4SNK5; -.
DR Proteomes; UP000019084; Unassembled WGS sequence.
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; IPR025902; LssY-like-C_dom.
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; PF14067; LssY_C; 1.
DR Pfam; PF01569; PAP2; 1.
DR Pfam; PF09335; SNARE_assoc; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..170
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 364..440
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|Pfam:PF01569"
FT DOMAIN 510..614
FT /note="LssY-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14067"
FT REGION 668..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 77823 MW; 0BA66DEA92C2F292 CRC64;
MPTYNRGMNS WIDATLEWIG HHPTLAGVVI FAIAFSDAVI VLGAIVPALP LLFAIGVLIG
LGQINGPYAV ACASLGAFVG DALSFWVGHR WGHQLHTYWP FRRYPQLLER GELLFRRNAF
KSILIARYVG AVRPFVPAIA GMSHMPFKRY LIASGLACIS WALLFLVPGW VLGTAYDAVA
AVAGRLFVVV ALLAAVIGLA WAMVLYSYRW SAGHLDALLA RLLEWSHRHP VLGNWSVSVF
DPRRRESVPL AMMALMLLLL GWGWFVLLMV VLAHGEPLRV DLAVHDLMLA LRNPLADYPM
VALASLGDWQ VLLPAIAAAM GYLAWRRRWM AVAHWVIALA FGLALTQLLG ATVQVVRPPA
ASNGFGFPSV AVTMATIGFG FFALLIAREL PGRRRVWPYL VSGAIVSLIG FARLYLGAHW
LSDVVGGMLF GIFWLLVLGI AYRRRATRAF WVKPVSWIFY GVFLTCAVVF APRNLGTKLA
RFEPPPPLLM ELPASDWWNG QWRLLPARRN EFDDDQRWPL DVQLAGPLAP LQRQLEARGW
RVQPQAGWEQ ALHLLDVSGR PDEVPILPAT LDTQVEALLM VRHAAPGHVH VLRLWPAAAR
LQPGAQPLWV GSTQTLRYSR HFSLIGLWYP LRGVDPALSA LRQALDPLPY RLEQRRRSQV
PVILIDSTSG NALRREDEDN AAPQTDTTAS DPAASGPSQQ RR
//
