ID   A0A1M6RN32_9BURK        Unreviewed;       645 AA.
AC   A0A1M6RN32;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferases {ECO:0000313|EMBL:SHK33865.1};
GN   ORFNames=SAMN05192548_101960 {ECO:0000313|EMBL:SHK33865.1};
OS   Paraburkholderia terricola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=169427 {ECO:0000313|EMBL:SHK33865.1, ECO:0000313|Proteomes:UP000184395};
RN   [1] {ECO:0000313|EMBL:SHK33865.1, ECO:0000313|Proteomes:UP000184395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20594 {ECO:0000313|EMBL:SHK33865.1,
RC   ECO:0000313|Proteomes:UP000184395};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FRAB01000019; SHK33865.1; -; Genomic_DNA.
DR   RefSeq; WP_073430071.1; NZ_JAVDRI010000010.1.
DR   AlphaFoldDB; A0A1M6RN32; -.
DR   STRING; 169427.SAMN05192548_101960; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000184395; 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:SHK33865.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:SHK33865.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        71..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        352..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          474..590
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   645 AA;  70750 MW;  E1DFFEBB58ED6C39 CRC64;
     MSDRPIPAGR RAARPHEAHE SQFRLLRQRR FAPFFWTQFL GAMNDNVFKI GFTSLVTYQA
     ARFSGVDPKT AAFLISAIFI LPFVLLSATS GQIADKYDKA MLTRFVKSFE IVVMLIGGAG
     FLLHNAPLLY ACTFLMGVHS TVFGPVKYSY LPQHLSKAEL VGGNGMVEMG TFVAILIGTI
     VGGAGAGFVE HGAIVLACAC VAVALAGRFV SSFVPVTAAP QPDLRINWNP VSETWRNLKL
     ARENRTVFLS LLGISWLWFV GATFLSSFFS FAKNVLSADP DVVTVLLGTF SIGIGIGSLL
     CEKLSKRRIE IGLVPLGSIG MSVFAIDLFF ASRALPPAGH LLAVGEFLVR PAHWRVLADL
     FLLAMFGGFY SVPLYALIQS RSQPSHRARI IAANNILNSL FMIVSALMAM ALTAAGFGIP
     AIFLVTALLN IVVATYIYSL VPEFLLRFIA WVLVHTFYRM RLVHAERIPE EGAAVLVCNH
     VSFVDAIVIM AESPRPIRFV MDHQIFRSPF AGWVFRHAKA IPIAPAHQDA QLLTQAYERC
     AQALAEGELV CIFPEGKLTR TGEMNPFRHG VTEIIRRTPA PVIPMALRGL WGSVFSRADD
     ARWPRPIQKG VMSRLTLAVG EPIDPALATP EMLQRIVTEL RGARK
//