ID A6DK79_9BACT Unreviewed; 1130 AA.
AC A6DK79;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=2-acyl-glycerophospho-ethanolamine acyltransferase {ECO:0000313|EMBL:EDM27777.1};
GN ORFNames=LNTAR_00210 {ECO:0000313|EMBL:EDM27777.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM27777.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM27777.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM27777.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(2010).
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:EDM27777.1}.
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DR EMBL; ABCK01000007; EDM27777.1; -; Genomic_DNA.
DR RefSeq; WP_007278292.1; NZ_ABCK01000007.1.
DR AlphaFoldDB; A6DK79; -.
DR STRING; 313628.LNTAR_00210; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000004947; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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; 3.30.300.30; -; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR24096:SF149; 4-COUMARATE--COA LIGASE 1-RELATED; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:EDM27777.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000004947};
KW Transferase {ECO:0000313|EMBL:EDM27777.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 435..549
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1130 AA; 123892 MW; B63A755081F9FC73 CRC64;
MTPQTRRLIP VAFANFFGTL NDNAFKNISI LIMAMSITDS SEELILNARI SIVFTVPFIL
FSVFAGWAGD RFCRHKVMGF AKACELPIML VGSVAVMLYD SSNPSPLLGG LLYSCVFLMA
VQSTFFVPAR ASIMPQLFNE QEIKDANGKL ELLNFAGIIL GTALAGVCVT YKASLLVLPI
FAIIGWFFIR KTQAVEAANP TLPFSLNPIK ELAGPMKTIR QDKGLLAAAI GETIFYSIGI
VLVFAILTMG KYDLMLSDIE RSLMLLPLTF GIGLGCFVAG RLNHTTMNRG LCVPGLMGMT
FALCQLISTS NPTIASLWIL LAGFFGGLFV LPIKVYLQEE TPEKERMRIM AAENILVFLG
MLFTTWLTYE FGKRSGDLTS HSVIWACSLA LALTCIPAAI ILSNNFLRLL VLGPIRLNYR
IRGRGLENVP HDGPLLLLPN HSTWIDGFLL SAAIPRNIVF MIDSTYYYKP LLKPFFEMFD
FLPVNTGRKS VLQSLEAGRQ ALADGKALCL FPEGVLTRSG FMNEFKSGFQ RVLKGNEDAT
VLPVYMGGTW DSTFSLRSGE RLSLTNTVGP LPPKISVHVG EVVPHDIPAL ELWEKVKELE
FIDHKIRADE NVPGPVKFLH HAKFNPFGSI FIDPDKGPIK NLPLLIKILA LSAKIKKVHG
KKEYTSILLP NTVAAVSSAL AAYYQDSVPV FLNSTVSKDG LAHALKTTDC QHVITSKLAI
KKMKIELPES CTPVYLEDIA KSITKVDVIK ALLSIARPSR SICKAKIDDT ATILFSSGST
GTPKGVELTH LNVSSNLDSL GMVCDLNQND VVLGHMPLFH AFGYLSAFYL PISQGTPAVM
QANPLDAKAV SENMGKYACS ILFATPSFLA NYTRRCKKED FSKLRLVLVG AEKLNANTSK
EFFEKFGVLP TEAYGATELA PGVSFNAPVK IWELGKKHLR DNSVGRPLPG IQIKTVNPDT
LEDLAHGEDG LLLVRSPGTM RGYLKDPDRT NAVLKNGWYI TGDIASIHRD GSIQLQGRLS
RFSKIAGEMV PHGAVEEVLH QEASTDPSQL AVMGVPDEAR GEKLIVLFTE LDKDIAEIIE
SLRSHGLPNL WIPRPQNFIQ IDEIPLLGSG KVDLKGLKDL AIKMVEKQNA
//
