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Database: UniProt
Entry: M9R068_9RHOB
LinkDB: M9R068_9RHOB
Original site: M9R068_9RHOB 
ID   M9R068_9RHOB            Unreviewed;       245 AA.
AC   M9R068;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:AGI65984.1};
GN   ORFNames=OAN307_c02170 {ECO:0000313|EMBL:AGI65984.1};
OS   Octadecabacter antarcticus 307.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI65984.1, ECO:0000313|Proteomes:UP000005307};
RN   [1] {ECO:0000313|EMBL:AGI65984.1, ECO:0000313|Proteomes:UP000005307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=307 {ECO:0000313|EMBL:AGI65984.1,
RC   ECO:0000313|Proteomes:UP000005307};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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DR   EMBL; CP003740; AGI65984.1; -; Genomic_DNA.
DR   RefSeq; WP_015498045.1; NC_020911.1.
DR   AlphaFoldDB; M9R068; -.
DR   STRING; 391626.OAN307_c02170; -.
DR   KEGG; oat:OAN307_c02170; -.
DR   eggNOG; COG0204; Bacteria.
DR   HOGENOM; CLU_027938_5_1_5; -.
DR   OrthoDB; 5290997at2; -.
DR   Proteomes; UP000005307; Chromosome.
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:AGI65984.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:AGI65984.1};
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          73..187
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   245 AA;  27105 MW;  8047DA6ECB6782D0 CRC64;
     MTYAIQWVRS LIFVGHMYFA MAVVGVVFFI PVICSRRAAI FACRFYCWWV QWAAGWMIGL
     KCEVRGTPPS DEVLVAGKHQ SFLDVIMIYG ALPTGKFIMK RILMYAPVLG QFGLRVGCIP
     VERGRRGMAI KKMVADVAAG RALPGQLIIY PQGTRIAPGV KAKYKVGAGI LYTELGQDCV
     PVAANVGVFW PKRGIYRAQG TAVIEFLPRI PAGMEMTAFT AKLEDVIETR SNELMREAGF
     TAIEE
//
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