ID   A0A261USZ7_9BORD        Unreviewed;       278 AA.
AC   A0A261USZ7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:OZI64785.1};
GN   ORFNames=CAL20_03830 {ECO:0000313|EMBL:OZI64785.1};
OS   Bordetella genomosp. 4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463044 {ECO:0000313|EMBL:OZI64785.1, ECO:0000313|Proteomes:UP000216885};
RN   [1] {ECO:0000313|EMBL:OZI64785.1, ECO:0000313|Proteomes:UP000216885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU9919 {ECO:0000313|EMBL:OZI64785.1,
RC   ECO:0000313|Proteomes:UP000216885};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OZI64785.1}.
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DR   EMBL; NEVQ01000003; OZI64785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261USZ7; -.
DR   OrthoDB; 9806880at2; -.
DR   Proteomes; UP000216885; 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:SF65; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 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:OZI64785.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216885};
KW   Transferase {ECO:0000313|EMBL:OZI64785.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          99..211
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   278 AA;  30337 MW;  489A99830FE38289 CRC64;
     MPASNHRYDA GRPPVRPVGG RDDGLGVLNL SLLKFPRIVL RLILVVLWII FGLLCVGLVY
     PFLGLSARAR LNRFWSRWLM SFCGIRVVVS GQPLLTGAVL WVANHVSWID IFVVNSVRAT
     SFVAKSEIRS WPVIGWLAAG AGTLFIERGQ RHAVHAVGEA VQARFQQGEA VGLFPEGTTS
     EGDTVRPFHA SLFEPARVAC IPIQPVVLRF LQHGQRSPLA AFVGEETLAT NLWRVLGATG
     LSVEVEFVAP LATQSPDGTP VTRLEISKHA RSAIADRL
//