ID L0WJK1_9GAMM Unreviewed; 293 AA.
AC L0WJK1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:EKF76010.1};
GN ORFNames=A11A3_00910 {ECO:0000313|EMBL:EKF76010.1};
OS Alcanivorax hongdengensis A-11-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF76010.1, ECO:0000313|Proteomes:UP000010164};
RN [1] {ECO:0000313|EMBL:EKF76010.1, ECO:0000313|Proteomes:UP000010164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-11-3 {ECO:0000313|EMBL:EKF76010.1,
RC ECO:0000313|Proteomes:UP000010164};
RX PubMed=23209226; DOI=10.1128/JB.01849-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT hongdengensis Type Strain A-11-3.";
RL J. Bacteriol. 194:6972-6972(2012).
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:EKF76010.1}.
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DR EMBL; AMRJ01000001; EKF76010.1; -; Genomic_DNA.
DR RefSeq; WP_008927373.1; NZ_AMRJ01000001.1.
DR AlphaFoldDB; L0WJK1; -.
DR STRING; 1177179.A11A3_00910; -.
DR PATRIC; fig|1177179.3.peg.177; -.
DR eggNOG; COG0204; Bacteria.
DR OrthoDB; 319710at2; -.
DR Proteomes; UP000010164; Unassembled WGS sequence.
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:EKF76010.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EKF76010.1};
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 TRANSMEM 118..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..226
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 293 AA; 33047 MW; 77ABBA9523DBE172 CRC64;
MGVLRGITGS ILLLLNTVVL IGPMMVLALL RLLVPGAAFK GACARGVMAI AETWAEICKA
IFALVTPTRW DIRCDEALSR DTSYLVVCNH QSWVDIPALV QTFNRKTPYF KFFLKKELIW
VPFLGLAFWA LDYPFMKRYS KAFLAKHPHL KGQDLEITRA ACEKFRGMPV TVVNFLEGTR
FTAAKHDRQQ SPYRHLLRPK AGGVAFVLAA LGDSLDALLD VTVVYPGGRT PGFWDLLCGR
VPRGIVDVRT RNLDAALWQG DYQSDPQARE RVQRWVSNLW AEKDRRLADL SRD
//
