ID D3HJB4_LEGLN Unreviewed; 405 AA.
AC D3HJB4;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Putative cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:CBJ12503.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:CBJ12503.1};
GN OrderedLocusNames=LLO_2113 {ECO:0000313|EMBL:CBJ12503.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ12503.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ12503.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ12503.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; FN650140; CBJ12503.1; -; Genomic_DNA.
DR RefSeq; WP_003636564.1; NC_013861.1.
DR AlphaFoldDB; D3HJB4; -.
DR STRING; 661367.LLO_2113; -.
DR KEGG; llo:LLO_2113; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_0_2_6; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000001060; Chromosome.
DR GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003333; CMAS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43667; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR PANTHER; PTHR43667:SF2; TUBERCULOSTEARIC ACID METHYLTRANSFERASE UFAA1; 1.
DR Pfam; PF02353; CMAS; 1.
DR PIRSF; PIRSF003085; CMAS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Methyltransferase {ECO:0000313|EMBL:CBJ12503.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBJ12503.1}.
FT ACT_SITE 385
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 405 AA; 46065 MW; BA525B8AAE81430B CRC64;
MDKNNHQSTQ SARLSKKVFF KLLNGITHGT IKVNDVNGSY VFGNENEKND SIASITINNP
KAYKAILVGG SVGAGASYIA GDWDTDDLQK LIEIIIKNDS LFNNIESPIA RLFNLIRTIH
YKLKFNSIRR AKENILAHYD LGNDFFKLIL DTSMMYSCAL YKPSEISLEE ASIKKIQAIC
TALQLKPSDH ILEIGTGWGG FACFAAQEYG CKVTTTTISE KQYLYVKDKI NQLNLNHQIE
LLKEDYRTLS GQYDKVVSIE MIEAVGHKYF DTFFHQCHQL LKPEGLFFLQ AIVINDQAYE
AAKNEVDFIK KYIFPGGCLP SVCSISQSIA SQTTLQLLSF EDIGHHYVST LNDWHKKLLA
NKQEICAQGF PESFIRTWEF YFCYCAAGFQ TNYISDIHAL WRKRR
//
