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Database: UniProt
Entry: A0A0W0YLM2_9GAMM
LinkDB: A0A0W0YLM2_9GAMM
Original site: A0A0W0YLM2_9GAMM 
ID   A0A0W0YLM2_9GAMM        Unreviewed;       332 AA.
AC   A0A0W0YLM2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Acylglycerophosphoethanolamine acyltransferase {ECO:0000313|EMBL:KTD57825.1};
GN   ORFNames=Lsha_2259 {ECO:0000313|EMBL:KTD57825.1};
OS   Legionella shakespearei DSM 23087.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD57825.1, ECO:0000313|Proteomes:UP000054600};
RN   [1] {ECO:0000313|EMBL:KTD57825.1, ECO:0000313|Proteomes:UP000054600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD57825.1,
RC   ECO:0000313|Proteomes:UP000054600};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD57825.1}.
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DR   EMBL; LNYW01000063; KTD57825.1; -; Genomic_DNA.
DR   RefSeq; WP_018577348.1; NZ_LNYW01000063.1.
DR   AlphaFoldDB; A0A0W0YLM2; -.
DR   STRING; 1122169.Lsha_2259; -.
DR   PATRIC; fig|1122169.6.peg.2600; -.
DR   eggNOG; COG0204; Bacteria.
DR   OrthoDB; 5645212at2; -.
DR   Proteomes; UP000054600; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10434:SF57; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:KTD57825.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW   Transferase {ECO:0000313|EMBL:KTD57825.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          79..200
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   332 AA;  37687 MW;  37848CD0F2CD1F3C CRC64;
     MFDNPEDQNS NLLNNAYWYL FALCSLMAMA YALTRYLERK NPFDYEHRST RAIVGLIRMF
     MLTLHTNSQE LAIPEDTSII AVGPHRSGAD ALALSVNMKG KPLRFWATDH YDKIPVVGPF
     MRTFKTIPVK ENTNRTAERT ANSDAIESAV KVVNENGRFA VFPQGNICYA GQDSPMIYNG
     TAIVAIRTQK PIVVLRLDGM SSIAPGLIPA FIKNSTYYRI FGTLLVPNDI RTTVCYTIDC
     HLKEPVSNLP EKEQLRHINA TLYAFFRHIK DLTPTQIEEI KKDINDGTHL QIWDKRDEMN
     TCQRQLKVLR AESKKLEDED SAKLFGAVAL RP
//
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