ID A0A0A1I1N9_9PSED Unreviewed; 479 AA.
AC A0A0A1I1N9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=clsA {ECO:0000256|HAMAP-Rule:MF_00190};
GN ORFNames=BN844_4324 {ECO:0000313|EMBL:CDF96440.1};
OS Pseudomonas sp. SHC52.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF96440.1, ECO:0000313|Proteomes:UP000031550};
RN [1] {ECO:0000313|EMBL:CDF96440.1, ECO:0000313|Proteomes:UP000031550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SHC52 {ECO:0000313|EMBL:CDF96440.1,
RC ECO:0000313|Proteomes:UP000031550};
RA Van der Voort M., Mendes R., Raaijmakers J.M.;
RT "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL Submitted (MAY-2013) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:CDF96440.1}.
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DR EMBL; CBLV010000320; CDF96440.1; -; Genomic_DNA.
DR RefSeq; WP_041023999.1; NZ_CBLV010000320.1.
DR AlphaFoldDB; A0A0A1I1N9; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000031550; 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; cd09155; PLDc_PaCLS_like_1; 1.
DR CDD; cd09161; PLDc_PaCLS_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 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT DOMAIN 218..245
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 392..419
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 223
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 230
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 397
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 399
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 404
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
SQ SEQUENCE 479 AA; 53865 MW; EBBCD19353F6A324 CRC64;
MDYFGPHIFG YLIALLHTLG SIAAVHAVLT VRTAQGSIAW ALSLVFIPYL TLIPYLVFGR
STFDGYIKAR RQANEEMRKA VSELNWRPWV EEALTARASQ AYDSLRAMPK LGRTPCLANN
EVRLLVNGHA TFEAIFQAIE SAREAVLIQF FIIHDDRLGQ RLQSLLLKKA AEGVAVYLLY
DRIGSHSLPH RYVQALRDGG VHVKAFATRS GWLNRFQVNF RNHRKIVTVD GVLGFVGGHN
VGDEYMGEMP PLSPWRDTHV EVRGPVVASM QESFAEDWFW AARSLPPLIL PDTYPDDGVL
CQLLASGPAD AQETCSLFFV EAIHAASERV WITTPYFIPD ESVFAALRLA VLRGVDVRIL
LPSRPDHKIV YAASSLYAFE AVRAGVRVFR YEPGFLHQKV VLIDREISAI GSANLDNRSF
RLNFEVMLLT VDIPFATEVE QMLEKDFAQA HEIAKEESRE THRLQKVGMR VARLISPIL
//
