ID A0A3S1B519_9BACL Unreviewed; 476 AA.
AC A0A3S1B519;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 13-SEP-2023, entry version 11.
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:RUT30608.1};
GN ORFNames=EJP77_12335 {ECO:0000313|EMBL:RUT30608.1};
OS Paenibacillus zeisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2496267 {ECO:0000313|EMBL:RUT30608.1, ECO:0000313|Proteomes:UP000272464};
RN [1] {ECO:0000313|EMBL:RUT30608.1, ECO:0000313|Proteomes:UP000272464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-5-3 {ECO:0000313|EMBL:RUT30608.1,
RC ECO:0000313|Proteomes:UP000272464};
RA Sun L., Chen Z.;
RL Submitted (DEC-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_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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:RUT30608.1}.
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DR EMBL; RZNX01000004; RUT30608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S1B519; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000272464; 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:SF20; CARDIOLIPIN SYNTHASE YWIE-RELATED; 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:UP000272464};
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 30..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 213..240
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 218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 220
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 225
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; 55437 MW; F256E5664008939A CRC64;
MLWLVFALIA FIFQSATILI LEFRNPSKTV AWLFILFCFP IIGFVLYYFV AQDYKKRKNL
RRRGTRLFQE MKGRLWRQAE IVESVQEMHN PEFHHQERLF NLLTHLSESP ITGCNRTKVL
TNGEDTYDAI LSEMENAKDH IHIEYYIFRS DEVGRRFKEV MIRKAREGVK IRMICDGLGS
YYLKNEFINE LKEAGIQFYF FLPPLIATID RRVNYRNHRK IVVIDGTIGF LGGINVGEDY
LGLYPKLGEW RDTHLQIEGD SIYFLQNTFL TDWRLASGER ISDPALFPEH HCTGNEQVQI
LTSGPDQHWD AIQEMCFEAI AVAKKRVWIT SPYFIPDPSV YTALKTAAVS GVEVKIIIPY
RSDSKLVHLA SLSYVEELLH AGVKFYQYTK GFIHAKVMIV DDLLATVGTA NMDMRSFFYN
FEMTAVLFDQ APIRRLMNDF EVDLTHCRPI SLREFSKRPR MQKGAEMLTR MLSPLL
//
