ID   A0A1I3RLC7_9FLAO        Unreviewed;      1222 AA.
AC   A0A1I3RLC7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=SAMN04487893_10894 {ECO:0000313|EMBL:SFJ47424.1};
OS   Myroides guanonis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Myroides.
OX   NCBI_TaxID=1150112 {ECO:0000313|EMBL:SFJ47424.1, ECO:0000313|Proteomes:UP000243887};
RN   [1] {ECO:0000313|Proteomes:UP000243887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26542 {ECO:0000313|Proteomes:UP000243887};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FORU01000008; SFJ47424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3RLC7; -.
DR   STRING; 1150112.SAMN04487893_10894; -.
DR   OrthoDB; 9803035at2; -.
DR   Proteomes; UP000243887; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR   InterPro; IPR004869; MMPL_dom.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR33406; MEMBRANE PROTEIN MJ1562-RELATED; 1.
DR   PANTHER; PTHR33406:SF2; MEMBRANE PROTEIN SCO6666-RELATED; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF03176; MMPL; 2.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243887};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        712..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        748..771
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        783..806
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        827..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          895..1005
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   1222 AA;  139681 MW;  FB2ACB01C5B04C0E CRC64;
     MENWFYKIYQ WGQKNKFLFY SCMLFLLLVS GWGAWNTKFE EDITRILPKS EESNVVVKLL
     DQLKFSDKIT VIIERESEGS TDEMVALATG FLDSLQSEKR FVKNIKGTVD DSSIQQTISF
     VYEHLPLFLE ENDYKLLDNK VHIDSIAPTV AANYRSLISP TSLVSKDFIQ KDPFGIGFIA
     LQKLQQLNVG GDFHIIDGFL FDKNETKLFL FIDPVYAGSE TKNNSIFIQK LNNLKAKLNQ
     DYAKRVSIDY FGASFVAVAN ADQIKQDIQK TVVISISVLM LLLMLFYRRI HIPFLLLVPT
     AISAIIALFI LYFIKDAISA ISLSIGAILI GITIDYALHI LTHYKHSGDI RVLYQDITKP
     IMMSATTTAI AFLCLVFVHS EALRDLGIFA AITVMGAGVF SLLLIPQLYT PSEKEIASAS
     RIKVLDRIAN FPFDTNKWVL GICLLTFGIS AFFINKVGFN NDLSTLNYFP EELKQAEQKL
     EQSLNSESKS LYLTCYGTDL DVILDENSVL YARLKEAKEE GLINQFSTLG DFVVSQKKQE
     EKIARWNAFW DRKNRKTIEE SFQKQGESFG FNKEAYQPFY DILSREYKPL NMMAFKTLNP
     QIIEEFYTEK EGHYTVSTLV KVSEDKRADF ISEFSNTERF MVIDRKEINE AFLGNIVKDF
     NSLVNYSIIA VFGIMWLFYR RIELALVGLI PIVITGFITA GLMGMFNIEF TIFSTIVCTL
     IFGQGVDFTI FMTSALQKEY TTGKNEMPLY RASILLAVLT TLLAIGTLVF AKHPALKSIS
     LVSIIGMSVA ALISFVLYPY IFRICFTNRQ RKGKSPISLR LLLHSSLSFI YFGLCGAFYS
     LVIRLVMILM PWSEKRKMIV FRKGMGMYMK SVLYSNPFVL KQVKNPYDER FEKPAILIAN
     HTSFLDSLVM GGMVHNKVAF LVNDWVYRSP VFGKAVQSAG FYPVSEGIDG SVDHLKKQLD
     FGFSLMVFPE GTRSRTNDIQ RFHKGAFFLA EQLQLDIIPV YIHGNSETIP KGDTVIYDGH
     IITTIGKRIA FDDDSFGKNY SERTKLIGRS FKKEFAVIRE NLEGVNYFKK KLFLAYLYKK
     PEIVKEVKKD FEKYSYHYYE LNKQLGSKDT IVHVGNDLGQ LDLLLVLQQS KRKVFSFISN
     EERRSVAQHT YVNQIRKLVY WDSLEVVPSA TLLISNLDEV IPLEYIKQFS KVILLKKEGV
     SLSLAPDYER VLENEFLEIW KL
//