ID A0A1Y0EK87_9BURK Unreviewed; 661 AA.
AC A0A1Y0EK87;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:ARU04053.1};
GN ORFNames=CCO03_04620 {ECO:0000313|EMBL:ARU04053.1};
OS Comamonas serinivorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1082851 {ECO:0000313|EMBL:ARU04053.1, ECO:0000313|Proteomes:UP000196138};
RN [1] {ECO:0000313|EMBL:ARU04053.1, ECO:0000313|Proteomes:UP000196138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26136 {ECO:0000313|EMBL:ARU04053.1,
RC ECO:0000313|Proteomes:UP000196138};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; CP021455; ARU04053.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0EK87; -.
DR KEGG; cser:CCO03_04620; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000196138; Chromosome.
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:ARU04053.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000196138};
KW Transferase {ECO:0000313|EMBL:ARU04053.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 470..591
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 661 AA; 71930 MW; CA746DC92F92624D CRC64;
MTESTRQAQA GQAPSGQFAL LGQRRFAPFF WTQFAGAAND NLFKFAFTVM VTYMLQVSWL
PADMAGLVIG ALFILPYLVF SATSGQLADK LEKRALIRFV KWLEVAIMAL AAWGFFSANV
PVLLLCTFLM GLHSTLFGPV KFAYLPQHLS ERELTGGNGM VEMGTFVAIL LGQLVGGVLV
VVPQVGPEWV GISCVVLALL GRLAAQFIPV SPATDPGLQV NWNPVTETWR NLRLAHEQLA
VFRSLLGISW MWFFGAVFLS QFPAFAKEVL HCDAHVASLL LAVFSVGIGV GALLCEKLSG
HQVEIGLVPV GAIGMTVFAI DLFFATRSLP APPASGLFDV GGFLQQGAHW RVMADLGLMS
MFTGLFSVPM YALIQLRARP SHRARIIAAN NILNALFMIA SAVIAGALLQ AGFSIPQIFL
FTGIANALVA AYIFFLVPEY WLRFHAWVLT KLVYRFRITG RDHIPADGPA VLIANHVSFI
DAVLLMAASP RPIRFIMDHQ IFKVPVLGWL FKLAKAIPIA PARDDPAAYE RAFVEAAQVL
REGELLAIFP EGAITRDGEL GAFKSGVLKI LEQARADGLS VPVVPMALTN LWGSYFSRIE
PTGAMTKPFR RGTFSPVGLS VGEAMPPEAQ TLETMRARVQ DLLQPATDGC RRHPDPTPSP
E
//
