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Database: UniProt
Entry: A0A119CWR1_THIDE
LinkDB: A0A119CWR1_THIDE
Original site: A0A119CWR1_THIDE 
ID   A0A119CWR1_THIDE        Unreviewed;       240 AA.
AC   A0A119CWR1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Acyl-phosphate glycerol 3-phosphate acyltransferase {ECO:0000313|EMBL:KVW97049.1};
GN   ORFNames=ABW22_06505 {ECO:0000313|EMBL:KVW97049.1};
OS   Thiobacillus denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW97049.1, ECO:0000313|Proteomes:UP000064243};
RN   [1] {ECO:0000313|EMBL:KVW97049.1, ECO:0000313|Proteomes:UP000064243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RG {ECO:0000313|EMBL:KVW97049.1,
RC   ECO:0000313|Proteomes:UP000064243};
RX   PubMed=26712544;
RA   Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA   van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT   "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT   Chemoautotroph.";
RL   Appl. Environ. Microbiol. 82:1486-1495(2015).
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:KVW97049.1}.
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DR   EMBL; LDUG01000018; KVW97049.1; -; Genomic_DNA.
DR   RefSeq; WP_059753531.1; NZ_LDUG01000018.1.
DR   AlphaFoldDB; A0A119CWR1; -.
DR   STRING; 1123392.GCA_000376425_01967; -.
DR   PATRIC; fig|36861.3.peg.772; -.
DR   OrthoDB; 9812274at2; -.
DR   Proteomes; UP000064243; 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:SF67; PHOSPHOLIPID_GLYCEROL ACYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 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:KVW97049.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW   Transferase {ECO:0000313|EMBL:KVW97049.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..185
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   240 AA;  26402 MW;  ECA90612B6268AB5 CRC64;
     MSLIRSLIFA VLQTTLTIFF SVVAFLSFPF SAHARYRLIT GYNHIVIWLA RWVLGIRYVV
     EGRENLPVQP AIILAKHQSA WETVAFLCLF PPVSPVIKQE LLNVPFFGWA FRMLSPIAID
     RGAGREALKQ IVAQGQEKLA QGFWVLVFPE GTRVAPGEKG RYGIGGGWLA ADTGAPIVPI
     AHNAGEVWPK NAFIKRPGTI TVRIGPVIDP TGKSAAELTR AVEAWIETEM TRLPPAAAHQ
//
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