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Database: UniProt
Entry: C4LGK9_CORK4
LinkDB: C4LGK9_CORK4
Original site: C4LGK9_CORK4 
ID   C4LGK9_CORK4            Unreviewed;       468 AA.
AC   C4LGK9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ACR16964.1};
DE            EC=2.1.1.79 {ECO:0000313|EMBL:ACR16964.1};
GN   Name=cfa1 {ECO:0000313|EMBL:ACR16964.1};
GN   OrderedLocusNames=ckrop_0172 {ECO:0000313|EMBL:ACR16964.1};
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR16964.1, ECO:0000313|Proteomes:UP000001473};
RN   [1] {ECO:0000313|EMBL:ACR16964.1, ECO:0000313|Proteomes:UP000001473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC   {ECO:0000313|Proteomes:UP000001473};
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC       {ECO:0000256|ARBA:ARBA00010815}.
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DR   EMBL; CP001620; ACR16964.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4LGK9; -.
DR   STRING; 645127.ckrop_0172; -.
DR   KEGG; ckp:ckrop_0172; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_6_2_11; -.
DR   Proteomes; UP000001473; 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; IPR020803; PKS_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43667; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR   PANTHER; PTHR43667:SF1; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR   Pfam; PF02353; CMAS; 1.
DR   PIRSF; PIRSF003085; CMAS; 1.
DR   SMART; SM00828; PKS_MT; 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:ACR16964.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001473};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACR16964.1}.
FT   DOMAIN          197..431
FT                   /note="Polyketide synthase methyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00828"
SQ   SEQUENCE   468 AA;  51591 MW;  8F177CD1FD31C892 CRC64;
     MVKIPGLARH ATSMVGADPT IMSALISTPL TKLIRPASHP MTVGEIIDAI ADFPIRVTAF
     DGSSAGGTNG AATSADASGD MGIHITKDGL AYIATAPGEL GLARAYLTDN LRVSGTHPAN
     PYDLFGVLRT VRLKKLSPST VRRIIGSLAA MDAFRNLPQP PQEMVPFWQR AIDGLSRHSQ
     QRDAESISHH YDVSNRFYEL FLGPSMTYTC AYYPDPSATL EEAQENKYRL IFDKLRLQPG
     DTLLDVGCGW GGMVRYAARH GVKAIGATLS REQAEWANEE IARQGLSDRA EVRFQDYRDI
     PETDFDAISA IGILEHIGTA NYHDFFSFLF NKLRPGGLIL NHCITRPINE AKTNAGPFLD
     RYIFPDGELH CSGNIIANMQ GAGFEVMHEE NLRPHYARTL KAWCNNLEEN WDAACEEVSE
     ATAKLYGVYM AGSAWGFDHN IVQLHQALGV KPLQDGTMAV PEHQWWES
//
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