ID A0A2Z2KAC7_9BACL Unreviewed; 471 AA.
AC A0A2Z2KAC7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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 Name=cls {ECO:0000313|EMBL:ASA19743.1};
GN ORFNames=B9T62_02310 {ECO:0000313|EMBL:ASA19743.1};
OS Paenibacillus donghaensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=414771 {ECO:0000313|EMBL:ASA19743.1, ECO:0000313|Proteomes:UP000249890};
RN [1] {ECO:0000313|EMBL:ASA19743.1, ECO:0000313|Proteomes:UP000249890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13049 {ECO:0000313|EMBL:ASA19743.1,
RC ECO:0000313|Proteomes:UP000249890};
RA Jung B.K., Hong S.-J., Shin J.-H.;
RT "Complete genome sequence of Paenibacillus donghaensis KCTC 13049T isolated
RT from East Sea sediment, South Korea.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP021780; ASA19743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2KAC7; -.
DR KEGG; pdh:B9T62_02310; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000249890; 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 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:UP000249890};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 212..239
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 385..411
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 217
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 219
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 224
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 390
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 392
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 397
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 471 AA; 54531 MW; 8A9AD732F2DA9D39 CRC64;
MLWIILAYSL LIIQIITIVI TEYRRPDKEA AWLVILFMIP LIGFLLYYFL SKKYTCHRIL
SQKEYSRRES FRADLIDRCN QRIPKNRLAE TVSKNNKIYT LLQNKQTLPI TACNETTVYT
EAEQAFKAIL ESIAMAKHHI HMEFYIIRDD NLGTQFKQLL IQKVQEGVNV RLLYDGIGSR
RLGKAFVKRL QQAGVEIGCF APPLTTFFNR QLNYRNHRKI VVVDGKIGFF GGLNIGDEYL
GKDPSFGYWR DTHFSMKGYA VLWIQYTFLT DWYTVKGQLL TDPTYYPIQE TQGKELVQIV
KSGPDETILE LIFSLIVSAK KRIYIETPYF VLDPSVLLAI KTAVMSGIDV RIIIPGIPDK
KLVYYCSLSY VQELLQAGVR FYCYQKGFLH AKVLISDDLA CAGSTNMDLR SFCDQFEMNA
VFFDGKVVNR LVEDFFTDLN VSQEIALSEF ERRPSLQKMK EVFARLLSPF F
//
