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Database: UniProt
Entry: F3G519_PSESJ
LinkDB: F3G519_PSESJ
Original site: F3G519_PSESJ 
ID   F3G519_PSESJ            Unreviewed;       297 AA.
AC   F3G519;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:EGH42169.1};
GN   ORFNames=PSYPI_07005 {ECO:0000313|EMBL:EGH42169.1};
OS   Pseudomonas syringae pv. pisi str. 1704B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH42169.1, ECO:0000313|Proteomes:UP000004986};
RN   [1] {ECO:0000313|EMBL:EGH42169.1, ECO:0000313|Proteomes:UP000004986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1704B {ECO:0000313|EMBL:EGH42169.1,
RC   ECO:0000313|Proteomes:UP000004986};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH42169.1}.
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DR   EMBL; AEAI01000341; EGH42169.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3G519; -.
DR   PATRIC; fig|629263.4.peg.1161; -.
DR   HOGENOM; CLU_054727_0_0_6; -.
DR   BioCyc; PSYR629263:G11X0-1280-MONOMER; -.
DR   Proteomes; UP000004986; Unassembled WGS sequence.
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:EGH42169.1};
KW   Transferase {ECO:0000313|EMBL:EGH42169.1}.
FT   DOMAIN          84..226
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   297 AA;  33753 MW;  8D261F91D4222CC4 CRC64;
     MRRLLTGCFV ALLLLINTLV LIGPLLVFAL LKLLFRGRMR DRCSAAVMWI AETWAEIDKV
     IFATCIPTQW DIRGDEGLRG DTSYLVISNH QSWVDIPALV QALNRRTPFF KFFLKKELIW
     VPLLGLAWWG LDYPFMKRYS KAFLAKHPQL KGKDLEITKA ACELFKRQPV TIVNYLEGTR
     FTAAKHAAQG SPYTHLLKPK AGGVAFVLAA MGEQLDAILD VTVVYPESGI PGFWDMLCGR
     VSNVIVDIRT RELDPALWQG DYENDPVFRE KVQGWVNQLW VEKDARIAAL RLELPGH
//
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