ID A0A0R2HYJ7_CARDV Unreviewed; 505 AA.
AC A0A0R2HYJ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=IV74_GL001127 {ECO:0000313|EMBL:KRN57872.1};
OS Carnobacterium divergens DSM 20623.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1449336 {ECO:0000313|EMBL:KRN57872.1, ECO:0000313|Proteomes:UP000051658};
RN [1] {ECO:0000313|EMBL:KRN57872.1, ECO:0000313|Proteomes:UP000051658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20623 {ECO:0000313|EMBL:KRN57872.1,
RC ECO:0000313|Proteomes:UP000051658};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN57872.1}.
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DR EMBL; JQBS01000001; KRN57872.1; -; Genomic_DNA.
DR RefSeq; WP_034568369.1; NZ_JQLO01000001.1.
DR AlphaFoldDB; A0A0R2HYJ7; -.
DR PATRIC; fig|1449336.4.peg.1152; -.
DR eggNOG; COG1502; Bacteria.
DR Proteomes; UP000051658; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051658};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 61..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 232..259
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 417..444
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 237
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 239
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 244
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 422
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 424
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 429
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 505 AA; 57653 MW; E75D19243A8A881B CRC64;
MKKIIQLFVI AGLIILIGHY LIILSSSLFI GASLITELVG IYIALRLLLF DSRSTNSKVA
WIAIIFILPI FGVICYFFFG RNPQNRLFTT AQKKEREKLI QRIHHLSDQL EELVVPKTSQ
RIESLTGIKA LNGNRLTLLT DGDETFSAIK RAIKQAKHHI HIQYYIYKSD ELGTELRDLL
IQKAREGVEV RFLYDGFGSK KLNTAFLTPM KQAGIEFYAY DPIFSIWISR TANLRNHRKI
IVIDGQIGFT GGLNVGNEYL GKVDRFKFWR DTHLMIEGNS VIELQEAFLY DWVYMENRKE
AANPFIKAEG IQHYFQPEAV GNEWVQVVYG GPYDQEKLVR DAMLDMIDSA EESVWITSPY
LVPDDESLAV LRRTAMSGVD VKILIPGKAD MALSFHGSNA YIETLLEAGA EVYSYRDDSF
IHGKMLLIDG KRGAIGTANF DIRSFRLNHE MMSFIYEASP ALDKMKANYI EDLENSYLNN
LEAMKQRSLI QKLKEQLASL FTPIL
//
