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Database: UniProt
Entry: B8FF01_DESAL
LinkDB: B8FF01_DESAL
Original site: B8FF01_DESAL 
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
//
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