ID F4KNV2_PORAD Unreviewed; 476 AA.
AC F4KNV2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 OrderedLocusNames=Poras_0557 {ECO:0000313|EMBL:AEE12510.1};
OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE12510.1, ECO:0000313|Proteomes:UP000006545};
RN [1] {ECO:0000313|Proteomes:UP000006545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC {ECO:0000313|Proteomes:UP000006545};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL Submitted (APR-2011) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01916}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01916}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01916}.
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DR EMBL; CP002689; AEE12510.1; -; Genomic_DNA.
DR RefSeq; WP_013760101.1; NC_015501.1.
DR AlphaFoldDB; F4KNV2; -.
DR STRING; 879243.Poras_0557; -.
DR KEGG; pah:Poras_0557; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_2_10; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000006545; Chromosome.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01916};
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:UP000006545};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 210..237
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 389..416
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 215
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 217
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 394
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 396
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 401
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 476 AA; 54648 MW; BA6C8024A1F9BFE3 CRC64;
MWTTVLTILY TLLVVGVVVV ILTGGDDIYR MFSWLMVVIF VPVAGVILYL LFGRSTASMR
LIPKDFLKKI NRMPVEHTDF DFHRATLENP DYSSLGKLLY NSDDRTVLAA SSMEVITVGT
DKYRQLFEDI RSAKQEIHLM YYIIMSDELG VELRDLLVDK AREGVKVRVV YDGLGSIRSD
LKGFWKPLRR AGGEVYAFLP VRFPFFNLRI NYRNHRKVVV IDQRIGYFGG MNVAQYYTQG
NELGQWRDTH FRIEGSAVAG LQRVFLVDWA VAVRKRFDLE PYFAKIDRGA SYEHPIAMQF
LTNGPQAHWQ TIEQAFIKAC SIAHEEILVQ TPYFLPPEGL LMSLCSAALR GVYVFVMLPE
RGDSYLTQRA SDSYLTQLLK AGVDVRRYRG GFLHSKLLVV DRRIVGIGSA NMDFRSLEIN
LEVMSFVYDK QIAEELSEAF EEDLKACRQL TLEEWSGRSF WIRTLEALAR LFSPLL
//
