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Database: UniProt
Entry: A0A239SHL0_9BURK
LinkDB: A0A239SHL0_9BURK
Original site: A0A239SHL0_9BURK 
ID   A0A239SHL0_9BURK        Unreviewed;       986 AA.
AC   A0A239SHL0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=TVP38/TMEM64 family inner membrane protein ydjZ {ECO:0000313|EMBL:SNU84897.1};
GN   Name=ydjZ {ECO:0000313|EMBL:SNU84897.1};
GN   ORFNames=SAMEA4530655_02208 {ECO:0000313|EMBL:SNU84897.1};
OS   Pandoraea sputorum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pandoraea.
OX   NCBI_TaxID=93222 {ECO:0000313|EMBL:SNU84897.1, ECO:0000313|Proteomes:UP000215126};
RN   [1] {ECO:0000313|EMBL:SNU84897.1, ECO:0000313|Proteomes:UP000215126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13161 {ECO:0000313|EMBL:SNU84897.1,
RC   ECO:0000313|Proteomes:UP000215126};
RG   Pathogen Informatics;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000798};
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DR   EMBL; LT906435; SNU84897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239SHL0; -.
DR   STRING; 93222.NA29_15260; -.
DR   Proteomes; UP000215126; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd09140; PLDc_vPLD1_2_like_bac_1; 1.
DR   CDD; cd09143; PLDc_vPLD1_2_like_bac_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   InterPro; IPR032816; VTT_dom.
DR   PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   Pfam; PF09335; SNARE_assoc; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        471..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        515..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        600..621
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        633..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        662..682
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          108..135
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          337..359
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          136..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..709
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   986 AA;  107932 MW;  2C1A95A13FC90DD3 CRC64;
     MRMLVDGEQY FSALREALLA ARHAVFILGW DIDSRMQLTP NKSDDGLPPG LRDFLDALVR
     RRKTLRIYCL SWDFAMLYAL EREWLPSVKL DWKTHRRLSF RLDGRHPTAA SHHQKVVVVD
     QRVAFVGGLD LTRNRWDTPA HAPDDPGRKD PSGHAYPPFH DVQAMVDGEA AYALAELAED
     RWHRATGKHV DLRLRTPRDA PYAPLDPWPV SVAPDLTEVD VAISRTAPAF EGRPAVHEIQ
     TLYLDAIASA RRRLYLENQY FTATCIGDAL IERLASPDCP DVAVVSRRAE SGWLQEQSMG
     VLRARLYRRL RDADPQARFR LYCPEVPGIA PACVNVHSKV MVVDDALLVI GSANLNNRSM
     ALDTECNLSV AANGDARIAA GIARARNRLL AEHLDVSEAA MAAALLRDEG LHEAIDELHR
     EGARTLSAFT PALKDADDAA SPGAVVLDPM EPIDFENVMG TFIETEARPL LAGRIVALVL
     LLLGLAGLAL AWRYTPLREW TDLPRVLRVV ERIRLMPFAP LVIMAVYLLG TLIMVPVTVL
     IIVTVVVFGP FAGAAYALAG TSLGAAAGYG VGRTLGRDAV QRFGGERLNA LSRQIGHHGL
     LAMVVLRLMP IAPFTLVNLV VGASRIRLRD CMLGTVIGML PGILIAAALV DRVAALAQRP
     NGWTAALLAA VLVLPGMGVV ALRRRIRGMG GETPEDDRPP RRSIDADVSS RPALRDVSSS
     RVETISREMS VASYNVHGCV GTDGVHSPDR IAQVLDEIDA DIVALQEIEA SATDVGTLAR
     LAAARDMHFI PGPTLRCGGQ DYGNAIMTRF APVAVRHIDL SVAGREPRAA IDATLAWEDP
     HGRETQLRVI ATHLGLRPGE RREQVQRLLE CLANQPGAAT VLMGDVNEWC LWGRPLRWLH
     RFFERAPHVA TFPSRWPLLA LDRIWTSPRA HLGAVRRHAT PLARRASDHL PLVSVLRITV
     PVSPRASARR DAETATQAVA AVAGGR
//
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