ID A0A3N4WGN7_9PAST Unreviewed; 487 AA.
AC A0A3N4WGN7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=EDC49_1643 {ECO:0000313|EMBL:RPE92345.1};
OS Frederiksenia canicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Frederiksenia.
OX NCBI_TaxID=123824 {ECO:0000313|EMBL:RPE92345.1, ECO:0000313|Proteomes:UP000276901};
RN [1] {ECO:0000313|EMBL:RPE92345.1, ECO:0000313|Proteomes:UP000276901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25797 {ECO:0000313|EMBL:RPE92345.1,
RC ECO:0000313|Proteomes:UP000276901};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-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_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:RPE92345.1}.
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DR EMBL; RKQT01000003; RPE92345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4WGN7; -.
DR Proteomes; UP000276901; 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 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT TRANSMEM 41..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT DOMAIN 220..247
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 400..427
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 227
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 232
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 405
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 407
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 412
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
SQ SEQUENCE 487 AA; 55723 MW; 8C738A04C28089A2 CRC64;
MNITVTQIAS IVSPLLFWFA IATVTLRLLT KKQSNSATIS WIMLIYLLPI VGLIIYLLFG
EITLGRKHAE KAQKLAPTYQ QWFTQLEQQP HLLRQNMSGR YLALFELCQR QLQIPCIAGN
ELKLFSSPDT IMRQIIRDIH QAQTEIRMIF YIWHNGGMVD EVAIALQQAA QRGVKVQILL
DAVGSADFIG SEHYHTMRSH GIEIAEALKV KLWRVFLSRI DLRQHRKIIV IDNHIAYTGS
MNMVDPAYFK QDQDVGQWID VMVRINGPVS TILAALHSWD WQIEEEIDAL PSLPDEKLLP
VEMDNQHAVQ ILPSGPNENK ELMPRALATA IYSARNSIVI TTPYFVPSPE IASALENAAL
RGVEVRIIVP ERNDSTMVEW ASRYFFDELL ETGVEIYRFE QGLLHTKSIV IDDRLVLIGS
VNMDIRSFLL NFEVTMIVDD KDFAKQVSLL QHDYIKASVQ IDAEKWAKRP VYQRITEKLF
YLSSPLL
//
