ID Q5QZD1_IDILO Unreviewed; 303 AA.
AC Q5QZD1;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Phosphate acyltransferase family protein {ECO:0000313|EMBL:AAV83401.1};
GN OrderedLocusNames=IL2569 {ECO:0000313|EMBL:AAV83401.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV83401.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV83401.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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DR EMBL; AE017340; AAV83401.1; -; Genomic_DNA.
DR RefSeq; WP_011235792.1; NC_006512.1.
DR AlphaFoldDB; Q5QZD1; -.
DR STRING; 283942.IL2569; -.
DR KEGG; ilo:IL2569; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_054727_0_0_6; -.
DR OrthoDB; 319710at2; -.
DR Proteomes; UP000001171; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR10983:SF16; LYSOCARDIOLIPIN ACYLTRANSFERASE 1; 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:AAV83401.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001171};
KW Transferase {ECO:0000313|EMBL:AAV83401.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..231
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 303 AA; 35456 MW; 8F69C9462A1FB328 CRC64;
MLTSILIPFR VVINFSWGLI TTAIIGVSII SIGIFKVLLP FKTPQRICSF LGNALFRVWA
YCMSMMFQLT QRMEWHIEGD LDIHEKGWYM VMANHRSWVD VLVLMHLTRR HMPMPRFFLK
SQLMWIPIIG WGCWVLDMPF MKRYSKELLE KKPHLKGKDI ATTTRSCAKF RHIPTTVVNF
CEGTRFTPEK HEKKQSPFRN LLPPKAGGTA FSLQIMGGQF EAILDITIVY PGTDKRPVVW
HLLSGQLKNV YVDIKTRPIT ADLIGDYASD EVFRAHFQQW LNQRWQEKDQ TIDEMRKQIH
STR
//
