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Database: UniProt
Entry: D2UBR9_XANAP
LinkDB: D2UBR9_XANAP
Original site: D2UBR9_XANAP 
ID   D2UBR9_XANAP            Unreviewed;       671 AA.
AC   D2UBR9;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Phosphatase PAP2 family protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=XALc_0773 {ECO:0000313|EMBL:CBA15291.1};
OS   Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA15291.1, ECO:0000313|Proteomes:UP000001890};
RN   [1] {ECO:0000313|EMBL:CBA15291.1, ECO:0000313|Proteomes:UP000001890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX   PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA   Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA   Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA   Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA   Rott P.;
RT   "The complete genome sequence of Xanthomonas albilineans provides new
RT   insights into the reductive genome evolution of the xylem-limited
RT   Xanthomonadaceae.";
RL   BMC Genomics 10:616-616(2009).
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; FP565176; CBA15291.1; -; Genomic_DNA.
DR   RefSeq; WP_012915301.1; NC_013722.1.
DR   AlphaFoldDB; D2UBR9; -.
DR   STRING; 380358.XALC_0773; -.
DR   GeneID; 57876090; -.
DR   KEGG; xal:XALC_0773; -.
DR   PATRIC; fig|29447.3.peg.772; -.
DR   eggNOG; COG0586; Bacteria.
DR   eggNOG; COG0671; Bacteria.
DR   OrthoDB; 9780918at2; -.
DR   Proteomes; UP000001890; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        329..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        359..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..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..164
FT                   /note="VTT"
FT                   /evidence="ECO:0000259|Pfam:PF09335"
FT   DOMAIN          358..435
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01569"
FT   DOMAIN          506..611
FT                   /note="LssY-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14067"
FT   REGION          645..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  74417 MW;  835077A6F35950B3 CRC64;
     MNVSWTDATL AWIAAHPMLA GAVIFAIALC DAVILLGTVV PALPLLFAIG VLIGLGRISG
     PYAVLSAALG ALIGDGLSYW VGYRWGHRLR SYWPFKRYPQ WLDRGEAMFR RNAFKSILVA
     RYVGAIRPFV PAVAGMLKMP LRRYLPPSSL AAVTWALLFL GPGWLLGQAY EAVAAVAGRL
     FLILGLLTLA LALVWTIVLH GYRWSAGHMD ALLARALDWS HRHPVIGRYS VAVFDPQRRE
     SVPLAMLATM LLVLGWGWFA LLMLVIAHDA PLRLDLAVHD LMLALRNPLA DAPMAALASL
     GDWQVLAPAT ALGLGYLTWR RRWMAATHWL AALAFGLALT KLLGSTVHVV QPPTASSGFG
     FPSVAVTMAT ISFGFFAVLI ARELPGRSRV WPYLLSGVVV TLIGFAHLYL GAHWLSDVVG
     GMLFGIFWLL VLGIAYRRRL ERRFWMTPLA WLFYGGFVVA ALCYAPRHLE RKLAKFEPPP
     PPLAQIATSA WWQHDWQQLP PRRNAFDDDQ RWPLNLQVAG PLAPLQRRLA AAGWRVQPQA
     GWRQALQLLD DTAIPAQVPV LPATLDTRVE SLLMLHHGAH SDELYALRLW PAAARLQPGN
     LPLWLGSVQR LRYERHFNLI GMWRPLPDTE SALDEVTDAL HDLPKRKEVH HSSQGSVLLV
     RSNDETPATR P
//
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