ID W8VI68_KLEPN Unreviewed; 406 AA.
AC W8VI68;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:AHM81611.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:AHM81611.1};
GN ORFNames=KPNJ2_04839 {ECO:0000313|EMBL:AHM81611.1};
OS Klebsiella pneumoniae 30684/NJST258_2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1420013 {ECO:0000313|EMBL:AHM81611.1, ECO:0000313|Proteomes:UP000019586};
RN [1] {ECO:0000313|EMBL:AHM81611.1, ECO:0000313|Proteomes:UP000019586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30684/NJST258_2 {ECO:0000313|EMBL:AHM81611.1};
RX PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J., Bonomo R.A.,
RA Musser J.M., Kreiswirth B.N.;
RT "Molecular dissection of the evolution of carbapenem-resistant multilocus
RT sequence type 258 Klebsiella pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CP006918; AHM81611.1; -; Genomic_DNA.
DR RefSeq; WP_025380807.1; NZ_CP006918.1.
DR AlphaFoldDB; W8VI68; -.
DR KEGG; kps:KPNJ2_04839; -.
DR PATRIC; fig|1420013.3.peg.4546; -.
DR HOGENOM; CLU_026434_0_2_6; -.
DR Proteomes; UP000019586; 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:AHM81611.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHM81611.1}.
FT ACT_SITE 387
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
SQ SEQUENCE 406 AA; 46909 MW; B5CBB0E3F73469EE CRC64;
MTDPVFALEP DVPRNVRLAR WLLFRLLSGL REGSLTVREG AQTFHFGDPA AALRAEARVC
TPEVYWRLLT GGSLAAAEAW MDGDWESHQL TALLQILARN GKVLGRLERG FRLLGKPVAR
LRHWTRRNTR AQARENIAAH YDLGNEFYAH FLDEDLLYSS ALFTDDQQDL TQAQRAKMAR
LCDQLALNPG DHLLEIGTGW GALAEYAARH YGCRVTTTTL SREQHRWATE RMARAGLQDR
VEVLLCDYRD LRGEYDKLVS VEMIEAVGQR YLPAFFRTCQ ARLRPGGRMA LQAITIQDQR
YRDYSKSVDF IQRYIFPGGF LPSITAMSEL MTRHTDFVVR NLFDMGPDYA RPLAHWRQRF
THAWQDIEKL GFDERFRRMW LYYFGYCEAG FNARTISVVQ LTAERV
//
