ID L1NN75_9FLAO Unreviewed; 483 AA.
AC L1NN75;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 13-SEP-2023, entry version 43.
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=HMPREF9078_02179 {ECO:0000313|EMBL:EKY04700.1};
OS Capnocytophaga sp. oral taxon 380 str. F0488.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1127693 {ECO:0000313|EMBL:EKY04700.1, ECO:0000313|Proteomes:UP000010436};
RN [1] {ECO:0000313|EMBL:EKY04700.1, ECO:0000313|Proteomes:UP000010436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0488 {ECO:0000313|EMBL:EKY04700.1,
RC ECO:0000313|Proteomes:UP000010436};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKY04700.1}.
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DR EMBL; AMES01000167; EKY04700.1; -; Genomic_DNA.
DR RefSeq; WP_009418933.1; NZ_KB291174.1.
DR AlphaFoldDB; L1NN75; -.
DR PATRIC; fig|1127693.3.peg.1975; -.
DR HOGENOM; CLU_038053_1_2_10; -.
DR Proteomes; UP000010436; 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}; 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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 217..244
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 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 224
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 229
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 401
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 403
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 408
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 483 AA; 55732 MW; C145825E82169947 CRC64;
MKFLLLYEIL YVLLIIVICL RIVWDTRSVS KALAYLLLVI FVPILGAIFY FSFGINYRKH
KIYHKKLTID QSFRQRLEQI YPQIRAHLNS LDTAFIAPYE KSLRFLSNIE ERLSIIPNEE
VKVICNGENL FPELLDALRA AKHHIHIEYY IYENDHIGNA IKNILIEKVR AGVEVRFIYD
DFGSQGIRKN IVKELLANGV PAFPFYKINF VKLANRMNYR NHRKIVVVDG YTAFVGGINI
SDKYNNEEPN ALYWRDTHLK VRGYSAHVLQ AVFLQDWNFC SEENVAIDAP YFPIVTQPYP
TDYFTQIVSS GADSDLSNIL FATVQLIYAA KREILITTPY FIPDTSLQEA LIIAALSGVE
VKLLVPKEGD SVFVHTASES FFEELLKAGV EIYRYEKGFV HAKTFVIDGE VASVGTANLD
ARSFDLNFEV NALVYNKEVA SDLRRIFYKD LEDASLLRLE AWEKRSKFKQ LIERIVRLFS
PFL
//
