ID B8FF01_DESAL Unreviewed; 315 AA.
AC B8FF01;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:ACL03678.1};
GN OrderedLocusNames=Dalk_1982 {ECO:0000313|EMBL:ACL03678.1};
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfatibacillaceae; Desulfatibacillum.
OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL03678.1, ECO:0000313|Proteomes:UP000000739};
RN [1] {ECO:0000313|EMBL:ACL03678.1, ECO:0000313|Proteomes:UP000000739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL03678.1,
RC ECO:0000313|Proteomes:UP000000739};
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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DR EMBL; CP001322; ACL03678.1; -; Genomic_DNA.
DR RefSeq; WP_012611107.1; NC_011768.1.
DR AlphaFoldDB; B8FF01; -.
DR KEGG; dal:Dalk_1982; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_054727_0_0_7; -.
DR Proteomes; UP000000739; 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:ACL03678.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW Transferase {ECO:0000313|EMBL:ACL03678.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
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 315 AA; 35995 MW; 5C57B6EE6081E63F CRC64;
MLSFLPATMR GCIHCILLGL NTLVVFSLLV PISILKLIIP IDAWRTFCAV ILKYIASGWV
AVNAFNGRFI NNIKWDVQGV DSLKSKDWYL VISNHQSWTD ILVLQTIFSR RIPFLKFFLK
KELIWVPVMG IAWWALDFPF MKRYSKAFLK KNPHLEGKDL ETTQKACEKF KKMPVSIVNY
VEGTRFTQEK HDRQNSPFKH LLKPKAGGIA FVMAAMGGQL HSLVNVTIAY PYGDKSFWDY
LCGRIAKITV RVETLPIAEE VQGDYFKDEL FRTRFQKWVN DLWVEKDALL DDLLSQEGKG
PEAADTNEEP AAAAG
//