ID Q2C3V1_9GAMM Unreviewed; 483 AA.
AC Q2C3V1;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 08-NOV-2023, entry version 58.
DE RecName: Full=Cardiolipin synthase A {ECO:0000256|HAMAP-Rule:MF_00190};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_00190};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_00190};
GN Name=cls {ECO:0000313|EMBL:EAR55676.1};
GN Synonyms=clsA {ECO:0000256|HAMAP-Rule:MF_00190};
GN ORFNames=SKA34_03249 {ECO:0000313|EMBL:EAR55676.1};
OS Photobacterium sp. SKA34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR55676.1, ECO:0000313|Proteomes:UP000005284};
RN [1] {ECO:0000313|EMBL:EAR55676.1, ECO:0000313|Proteomes:UP000005284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA34 {ECO:0000313|EMBL:EAR55676.1,
RC ECO:0000313|Proteomes:UP000005284};
RA Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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_00190}.
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_00190};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00190};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00190}. 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. ClsA sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00190}.
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:EAR55676.1}.
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DR EMBL; AAOU01000015; EAR55676.1; -; Genomic_DNA.
DR RefSeq; WP_006646984.1; NZ_CH724144.1.
DR AlphaFoldDB; Q2C3V1; -.
DR HOGENOM; CLU_038053_1_0_6; -.
DR OrthoDB; 9814092at2; -.
DR Proteomes; UP000005284; 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; cd09152; PLDc_EcCLS_like_1; 1.
DR CDD; cd09158; PLDc_EcCLS_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR HAMAP; MF_00190; Cardiolipin_synth_ClsA; 1.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR030840; CL_synthase_A.
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_00190};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00190};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00190};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00190}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00190}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT TRANSMEM 35..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT DOMAIN 219..246
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 396..423
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 224
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 226
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 401
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 403
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 408
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
SQ SEQUENCE 483 AA; 54844 MW; E85651A13643FD34 CRC64;
MEQFYQVLTW IGVFAYWLLI ASVTVRVVFK RRVVGVSLAW MMIIYIVPIG GVIAYLLFGE
LNLGKKRAER AREMFLPFGN WFKQLNDCPG HQPQQMSLVA KPISELCENR LGIPGLIGND
LSLQSSPQEI LRSLVNDINH AQYSIHLEFY IWNPGGLADE VGVALIQAAK RDVKVRLLLD
SAGSMRFFQS HWPKLMRGAG IELVEALAVS PFRMFFRRLD LRLHRKIVVV DDHIAYTGSM
NLVDPSFFKV DAGVGQWVDV MVRISGPTVS VLNCIQAWDW EVETGKRFLP PLPSCTFDTA
HKDTVQVIPS GPGMPDDIIH QALLLSIYQA QKSVVITTPY FVPSEHLLHA MKGAADRGIA
VHIVIPRKND SVMVEWASRS FFSDLLESGV HIHRFHGGLL HTKSVVIDDS HCLIGTVNLD
MRSLWLNFEV TMAVDNIDFT QELSQLQQTY IADSDEIDRE QWSKRSMKNK FIERFFYMFS
PLL
//
