ID I6E1C4_SHIBO Unreviewed; 473 AA.
AC I6E1C4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Cardiolipin synthase C {ECO:0000256|HAMAP-Rule:MF_01918};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01918};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01918};
GN Name=clsC {ECO:0000256|HAMAP-Rule:MF_01918};
GN ORFNames=SB444474_2330 {ECO:0000313|EMBL:EIQ37816.1};
OS Shigella boydii 4444-74.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=766140 {ECO:0000313|EMBL:EIQ37816.1, ECO:0000313|Proteomes:UP000004199};
RN [1] {ECO:0000313|EMBL:EIQ37816.1, ECO:0000313|Proteomes:UP000004199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4444-74 {ECO:0000313|EMBL:EIQ37816.1,
RC ECO:0000313|Proteomes:UP000004199};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of cardiolipin (CL)
CC (diphosphatidylglycerol) from phosphatidylglycerol (PG) and
CC phosphatidylethanolamine (PE). {ECO:0000256|HAMAP-Rule:MF_01918}.
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:0000256|HAMAP-Rule:MF_01918};
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsC sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01918}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIQ37816.1}.
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DR EMBL; AKNB01000237; EIQ37816.1; -; Genomic_DNA.
DR AlphaFoldDB; I6E1C4; -.
DR PATRIC; fig|766140.3.peg.2455; -.
DR Proteomes; UP000004199; Unassembled WGS sequence.
DR GO; GO:0090483; F:phosphatidylglycerol-phosphatidylethanolamine phosphatidyltransferase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09111; PLDc_ymdC_like_1; 1.
DR CDD; cd09113; PLDc_ymdC_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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 PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF12; CARDIOLIPIN SYNTHASE C; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01918};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01918};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01918};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01918};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01918}.
FT DOMAIN 125..152
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 364..391
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01918"
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01918"
FT ACT_SITE 137
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01918"
FT ACT_SITE 369
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01918"
FT ACT_SITE 371
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01918"
FT ACT_SITE 376
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01918"
SQ SEQUENCE 473 AA; 53666 MW; CF7D856D10300CD6 CRC64;
MPRLASAVLP LCSQHPGQCG LFPLEKSLDA FAARYRLAEM AEHTLDVQYY IWQDDMSGRL
LFSALLAAAK RGVRVRLLLD DNNTPGLDDI LRLLDSHPRI EVRLFNPFSF RLLRPLGYIT
DFSRLNRRMH NKSFTVDGVV TLVGGRNIGD AYFGAGEEPL FSDLDVMAIG PVVEDVADDF
ARYWYCKSVS PLQQVLDVPE GEMADRIELP ASWHNDAMTH RYLRQMESSP 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
//
