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Database: UniProt
Entry: A0A0Q6MDD4_9BURK
LinkDB: A0A0Q6MDD4_9BURK
Original site: A0A0Q6MDD4_9BURK 
ID   A0A0Q6MDD4_9BURK        Unreviewed;       629 AA.
AC   A0A0Q6MDD4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:KQU78078.1};
GN   ORFNames=ASC88_19820 {ECO:0000313|EMBL:KQU78078.1};
OS   Rhizobacter sp. Root29.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU78078.1, ECO:0000313|Proteomes:UP000051195};
RN   [1] {ECO:0000313|EMBL:KQU78078.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU78078.1,
RC   ECO:0000313|Proteomes:UP000051195};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU78078.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU78078.1,
RC   ECO:0000313|Proteomes:UP000051195};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KQU78078.1}.
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DR   EMBL; LMCN01000009; KQU78078.1; -; Genomic_DNA.
DR   RefSeq; WP_056803193.1; NZ_LMCN01000009.1.
DR   AlphaFoldDB; A0A0Q6MDD4; -.
DR   STRING; 1736511.ASC88_19820; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000051195; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   CDD; cd06173; MFS_MefA_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR43266:SF2; LYSOPHOSPHOLIPID TRANSPORTER LPLT; 1.
DR   PANTHER; PTHR43266; MACROLIDE-EFFLUX PROTEIN; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:KQU78078.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051195};
KW   Transferase {ECO:0000313|EMBL:KQU78078.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        404..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          459..575
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   629 AA;  68324 MW;  62074D43567344A6 CRC64;
     MDPHAHPNQF ALLGQRRFAP FFWTQFLGAG NDNLFKFAFT VLVTYKVQVS WLSPQLAGLV
     IGALFILPFL LFSATSGQLT DKYDKTRVIQ LVKSLEIAIM LLAAWGFWAT HVPVLLACVF
     LMGLHSTLFG PVKFAYLPQH LGERELTGGN GMVEMGTFVA ILLGQVAGGL LVGIPEVGRH
     YVAIGCVAVA LLGRLTAQYV PPSPSTDPGL KINWNPVTET WRNLKLANQN VAVFRSLLGI
     SWMWFFGAAF LSLFPAFAKE VLHGDEQVAS LLLVVFSIGI GTGSLLCEVV SRRHVEIGLV
     PLGAIGMSIF AIDLFFASRG LPPSAQLSLA GFVSVGAHWR VMADLALLSL FAGLYSVPMY
     AMIQLRSQPS HRARIIAANN ILNALFMIVS AVLVGALLKA GLSIPQVFLI VGVLNAVVAF
     YIFLVVPEYL LRFIALVATR CIYRFKVRGD EHIPLKGAAI LVCNHVSFVD AVLLMAASPR
     PIAFIMDHRI FKLPVLGWMF KLAKAIPIAP QRENAQVYEQ AFERARAVLA DGELVCIFPE
     GAITKDGQLG EFKGGVMKLL ETHPVPVIPL ALQNLWGSFF SRVEQGGAMV KPFRRGLFSR
     VGMVAGAPLA AGDVTPDGLR TRVGELLAS
//
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