CLSC_ECOLI
ID CLSC_ECOLI Reviewed; 473 AA.
AC P75919;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cardiolipin synthase C {ECO:0000255|HAMAP-Rule:MF_01918};
DE Short=CL synthase {ECO:0000255|HAMAP-Rule:MF_01918};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01918};
GN Name=clsC {ECO:0000255|HAMAP-Rule:MF_01918, ECO:0000303|PubMed:22988102};
GN Synonyms=ymdC; OrderedLocusNames=b1046, JW5150;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DISRUPTION PHENOTYPE,
RP MUTAGENESIS OF HIS-130 AND HIS-369, AND GENE NAME.
RX PubMed=22988102; DOI=10.1073/pnas.1212797109;
RA Tan B.K., Bogdanov M., Zhao J., Dowhan W., Raetz C.R., Guan Z.;
RT "Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and
RT phosphatidylglycerol as substrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16504-16509(2012).
CC -!- FUNCTION: Catalyzes the synthesis of cardiolipin (CL)
CC (diphosphatidylglycerol) from phosphatidylglycerol (PG) and
CC phosphatidylethanolamine (PE). {ECO:0000269|PubMed:22988102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine = a cardiolipin +
CC ethanolamine; Xref=Rhea:RHEA:42972, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64612, ChEBI:CHEBI:64716;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01918,
CC ECO:0000269|PubMed:22988102};
CC -!- ACTIVITY REGULATION: Full activity requires coexpression with the
CC neighboring gene ymdB. {ECO:0000269|PubMed:22988102}.
CC -!- DISRUPTION PHENOTYPE: Triple deletion of clsA, clsB and clsC results in
CC a complete lack of cardiolipin, regardless of growth phase or growth
CC conditions. {ECO:0000269|PubMed:22988102}.
CC -!- MISCELLANEOUS: All three cardiolipin synthases (ClsA, ClsB and ClsC)
CC contribute to CL synthesis in stationary phase. Only ClsA contributes
CC to synthesis during logarithmic growth phase.
CC {ECO:0000305|PubMed:22988102}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_01918}.
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DR EMBL; U00096; AAC74130.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35836.2; -; Genomic_DNA.
DR PIR; C64847; C64847.
DR RefSeq; NP_415564.2; NC_000913.3.
DR AlphaFoldDB; P75919; -.
DR BioGRID; 4260689; 12.
DR BioGRID; 851648; 1.
DR DIP; DIP-12712N; -.
DR IntAct; P75919; 1.
DR STRING; 511145.b1046; -.
DR jPOST; P75919; -.
DR PaxDb; P75919; -.
DR PRIDE; P75919; -.
DR EnsemblBacteria; AAC74130; AAC74130; b1046.
DR EnsemblBacteria; BAA35836; BAA35836; BAA35836.
DR GeneID; 947321; -.
DR KEGG; ecj:JW5150; -.
DR KEGG; eco:b1046; -.
DR PATRIC; fig|511145.12.peg.1087; -.
DR EchoBASE; EB3634; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_026287_0_0_6; -.
DR InParanoid; P75919; -.
DR OMA; THRYLRQ; -.
DR PhylomeDB; P75919; -.
DR BioCyc; EcoCyc:G6551-MON; -.
DR BioCyc; MetaCyc:G6551-MON; -.
DR BRENDA; 2.7.8.B11; 2026.
DR PRO; PR:P75919; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0090483; F:phosphatidylglycerol-phosphatidylethanolamine phosphatidyltransferase activity; IDA:EcoCyc.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:EcoCyc.
DR HAMAP; MF_01918; Cardiolipin_synth_ClsC; 1.
DR InterPro; IPR030871; Cardiolipin_synth_ClsC.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13091; PLDc_2; 2.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Transferase.
FT CHAIN 1..473
FT /note="Cardiolipin synthase C"
FT /id="PRO_0000201289"
FT DOMAIN 125..152
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01918"
FT DOMAIN 364..391
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01918"
FT ACT_SITE 130
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01918"
FT ACT_SITE 132
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01918"
FT ACT_SITE 137
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01918"
FT ACT_SITE 369
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01918"
FT ACT_SITE 371
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01918"
FT ACT_SITE 376
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01918"
FT MUTAGEN 130
FT /note="H->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22988102"
FT MUTAGEN 369
FT /note="H->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22988102"
SQ SEQUENCE 473 AA; 53666 MW; C98F856D1FD00CD6 CRC64;
MPRLASAVLP LCSQHPGQCG LFPLEKSLDA FAARYRLAEM AEHTLDVQYY IWQDDMSGRL
LFSALLAAAK RGVRVRLLLD DNNTPGLDDI LRLLDSHPRI EVRLFNPFSF RLLRPLGYIT
DFSRLNRRMH NKSFTVDGVV TLVGGRNIGD AYFGAGEEPL FSDLDVMAIG PVVEDVADDF
ARYWYCKSVS PLQQVLDVPE GEMADRIELP ASWHNDAMTH RYLRKMESSP FINHLVDGTL
PLIWAKTRLL SDDPAKGEGK AKRHSLLPQR LFDIMGSPSE RIDIISSYFV PTRAGVAQLL
RMVRKGVKIA ILTNSLAAND VAVVHAGYAR WRKKLLRYGV ELYELKPTRE QSSTLHDRGI
TGNSGASLHA KTFSIDGKTV FIGSFNFDPR STLLNTEMGF VIESETLAQL IDKRFIQSQY
DAAWQLRLDR WGRINWVDRH AKKEIILKKE PATSFWKRVM VRLASILPVE WLL
