ID   CFA_ECOL6               Reviewed;         382 AA.
AC   P0A9H8; P30010;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cyclopropane-fatty-acyl-phospholipid synthase;
DE            Short=CFA synthase;
DE            Short=Cyclopropane fatty acid synthase;
DE            EC=2.1.1.79;
GN   Name=cfa; OrderedLocusNames=c2055;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Transfers a methylene group from S-adenosyl-L-methionine to
CC       the cis double bond of an unsaturated fatty acid chain resulting in the
CC       replacement of the double bond with a methylene bridge. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-
CC         methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid
CC         + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN80515.1; -; Genomic_DNA.
DR   RefSeq; WP_000098896.1; NC_004431.1.
DR   AlphaFoldDB; P0A9H8; -.
DR   SMR; P0A9H8; -.
DR   STRING; 199310.c2055; -.
DR   EnsemblBacteria; AAN80515; AAN80515; c2055.
DR   KEGG; ecc:c2055; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_6_0_6; -.
DR   OMA; LHCITAQ; -.
DR   BioCyc; ECOL199310:C2055-MON; -.
DR   SABIO-RK; P0A9H8; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR003333; Mycolic_cyclopropane_synthase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PIRSF; PIRSF003085; CMAS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..382
FT                   /note="Cyclopropane-fatty-acyl-phospholipid synthase"
FT                   /id="PRO_0000089571"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000250"
FT   BINDING         137..138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         171..179
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         197..202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  43909 MW;  861FF3314FDAF2C4 CRC64;
     MSSSCIEEVS VPDDNWYRIA NELLSRAGIA INGSAPADIR VKNPDFFKRV LQEGSLGLGE
     SYMDGWWECD RLDMFFSKVL RAGLENQLPH HFKDTLRIAG ARLFNLQSKK RAWIVGKEHY
     DLGNDLFSRM LDPFMQYSCA YWKDADNLES AQQAKLKMIC EKLQLKPGMR VLDIGCGWGG
     LAHYMASNYD VSVVGVTISA EQQKMAQERC EGLDVTILLQ DYRDLNDQFD RIVSVGMFEH
     VGPKNYDTYF AVVDRNLKPE GIFLLHTIGS KKTDLNVDPW INKYIFPNGC LPSVRQIAQS
     SEPHFVMEDW HNFGADYDTT LMAWYERFLA AWPEIADNYS ERFKRMFTYY LNACAGAFRA
     RDIQLWQVVF SRGVENGLRV AR