ID A0A2V4WYK4_9FLAO Unreviewed; 484 AA.
AC A0A2V4WYK4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Cardiolipin synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01916};
GN ORFNames=DFQ11_101161 {ECO:0000313|EMBL:PYE82736.1};
OS Winogradskyella epiphytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=262005 {ECO:0000313|EMBL:PYE82736.1, ECO:0000313|Proteomes:UP000248054};
RN [1] {ECO:0000313|EMBL:PYE82736.1, ECO:0000313|Proteomes:UP000248054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7945 {ECO:0000313|EMBL:PYE82736.1,
RC ECO:0000313|Proteomes:UP000248054};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC Rule:MF_01916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a
CC cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01916};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01916};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01916}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01916}.
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:PYE82736.1}.
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DR EMBL; QJTD01000001; PYE82736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4WYK4; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000248054; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09110; PLDc_CLS_1; 1.
DR CDD; cd09112; PLDc_CLS_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR HAMAP; MF_01916; Cardiolipin_synth_Cls; 1.
DR InterPro; IPR030874; Cardiolipin_synth_Firmi.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR NCBIfam; TIGR04265; bac_cardiolipin; 1.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01916};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_01916};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_01916}; Reference proteome {ECO:0000313|Proteomes:UP000248054};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01916}.
FT TRANSMEM 5..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 215..242
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 397..424
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 220
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 227
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 402
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 404
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 409
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 484 AA; 55993 MW; E9FAF037B45F62D0 CRC64;
MNWIIIGEIL YILLMIFVIS RALYETRSST KALAYILFII FVPFIGMIFY FTFGINYRKR
KLYSKKIVKD EPLRARIRNR MNTYSEQIRK SGLIREKHRN LIEYIRLAGS SPLTASNDVK
LLINGEEKFP ELLKALESAT SHIHIEYYIY EDDITGNQIA DMLIKKAKEG VEVRFMYDDF
GSHSLRRSFI NRLNEAGIQT APFYKIKWYA FANRLNYRNH RKIVIIDGIV SFIGGINMSD
KYRNDLKEKD PLFWRDTHLM IKGQATAYLQ YLFMCDWNFS SATNMEYSPT YFPDHTETMD
IENKVVQFAA SGPDSVQPVI FYSLLEAINS ARQSIYITSP YFIPGESLMD ALIIAIQCGL
DVKIIIPGVS DSKLVDAAAS AYYTELLQYG AKIYKYNKGF VHAKTMVIDN VLAVVGSANM
DYRSFDLNFE VNAMVYSETL AQQLTSAFED DLKESELIDG EMWLNRPTYI HLWEKTVRLL
SPFL
//
