ID A0A163Z9Y0_9FLAO Unreviewed; 1220 AA.
AC A0A163Z9Y0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glycerol acyltransferase {ECO:0000313|EMBL:KZE81347.1};
GN ORFNames=AV926_08675 {ECO:0000313|EMBL:KZE81347.1},
GN SAMN04488018_102363 {ECO:0000313|EMBL:SEI63629.1};
OS Myroides marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=703342 {ECO:0000313|EMBL:KZE81347.1, ECO:0000313|Proteomes:UP000076630};
RN [1] {ECO:0000313|EMBL:KZE81347.1, ECO:0000313|Proteomes:UP000076630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L41 {ECO:0000313|EMBL:KZE81347.1,
RC ECO:0000313|Proteomes:UP000076630};
RA Hong K.W.;
RT "Whole genome sequencing of Myroides marinus L41.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SEI63629.1, ECO:0000313|Proteomes:UP000183077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23048 {ECO:0000313|EMBL:SEI63629.1,
RC ECO:0000313|Proteomes:UP000183077};
RA de Groot N.N.;
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; LQNU01000053; KZE81347.1; -; Genomic_DNA.
DR EMBL; FNYS01000002; SEI63629.1; -; Genomic_DNA.
DR RefSeq; WP_038985562.1; NZ_LQNU01000053.1.
DR AlphaFoldDB; A0A163Z9Y0; -.
DR GeneID; 82256053; -.
DR OrthoDB; 9803035at2; -.
DR Proteomes; UP000076630; Unassembled WGS sequence.
DR Proteomes; UP000183077; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; 1.
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 Acyltransferase {ECO:0000313|EMBL:KZE81347.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:KZE81347.1};
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 268..287
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..340
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 437..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..678
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 711..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 747..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 894..1003
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1220 AA; 138975 MW; B2D9AD74E298ADE9 CRC64;
MSSVFYHIYK WGEKNKVIFF ILSILFVVLT AYGALNIKFE EDITRILPKN EKTSITSKIL
GQLRFSDKVS VIIEKQKDGT TDDMVELANQ FLDSLAVKNE YVKSIQGKVD DENINEAISF
VYDHLPLFLE ETDYDKIATK LNNDSLKQVV EGNYKTLISP TGMVAKQFIQ RDPMGIGFMA
LQKLQQLNIG DDFHLVDGYI MNKDEDKLLL FIDPVYDGTE TEHNTIFVNY LNGVKEDLNK
TYLDKVSVDY FGASFVAVAN AKQIKSDIQK TVAISVTVLM LLLIAFYRKL FIPIILFIPT
VFAALVALFV LYFIKDSISA ISLSVGAILI GITIDYALHI MTHYKHSGDI KEVYREITRP
IIMSCATTAI AFLCLVFVHS EALKDLGIFA SITVMAAGIF SLLFIPHLYK PSAKDLVGES
STVLDKVAKY PFDKSKWLLG LCLLAIVVSC FAFNHTIFNK DLSSMNYFPE ELKQAEEKLN
NTLDSNSKSL YITCYGEDVD EVVEDNARLA QHLQLEQSEG NILQYSSLGN IVLSKSQQEQ
KIKRWNEFWA KQDITALKST LIREGLKYDF MESTYTGFYN LLATSFSVIP IQEYVKLNPQ
IMDEFFIEKD GFYTINTLVK VKESDRATFV NALKGPKEYL VIDRKAINET FLSNLVNDFT
SLVNYSFIAV LLILWFFFRR AEMVIVSMIP IMITGFITTG LMGLFQIEFN IFSSIVCTLV
FGQGVDFTIF MTNALQKEYT TGKDESVMYR SSIILAVLTT LLAIGTLIFA KHPALRSISM
VSLIGLSVSA IVAFVLYPRL YRFCFTNRQR KGLSPITLRL TLFSVVSFTY FGLFGILYSC
IARVLMLILP MPKVVKLRWF GKGMSLYQTS VLYLNPFVKK GIINKHKEDF KKPAIIIANH
TSFLDSLTIG MVNSNIVYLV NDWVYKSPIF GRAVQMAGFY PVSNGVDNSV AHLEERVKQG
FSLMIFPEGT RSMTNDVQRF HKGAFFLAET LKLDILPMYI HGNSEVIPKG DYVIYGGHII
TTVGERIAYD DSSYGSNYAE RTKKISRFFK EQFKEIRTEL EDKNYFRRKL LLSYYYKEGN
ILKEVKEDFK QYADDYYELN NHLSDKEKIV HLGDDYGQIN FLVTLQQSKR KVYAYLSDSY
KRSVAQTNYV TKCRSVVYVE DIDAVDSSVT TLLVSAAVEH SVGEHINKIV VLRRKTNGYE
PEHGFDLAVE NEYISVYLRK
//
