ID A0A3G9JD89_9BACL Unreviewed; 484 AA.
AC A0A3G9JD89;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=clsA {ECO:0000313|EMBL:BBH22933.1};
GN ORFNames=Back11_42780 {ECO:0000313|EMBL:BBH22933.1}, FHS14_000995
GN {ECO:0000313|EMBL:MBB3068019.1};
OS Paenibacillus baekrokdamisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1712516 {ECO:0000313|EMBL:BBH22933.1, ECO:0000313|Proteomes:UP000275368};
RN [1] {ECO:0000313|EMBL:BBH22933.1, ECO:0000313|Proteomes:UP000275368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 33723 {ECO:0000313|EMBL:BBH22933.1,
RC ECO:0000313|Proteomes:UP000275368};
RA Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA Lee J.S.;
RT "Complete genome sequence of Paenibacillus baekrokdamisoli strain KCTC
RT 33723.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3068019.1, ECO:0000313|Proteomes:UP000562277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8890 {ECO:0000313|EMBL:MBB3068019.1,
RC ECO:0000313|Proteomes:UP000562277};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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; AP019308; BBH22933.1; -; Genomic_DNA.
DR EMBL; JACHXC010000002; MBB3068019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9JD89; -.
DR KEGG; pbk:Back11_42780; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000275368; Chromosome.
DR Proteomes; UP000562277; 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:UP000275368};
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 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 33..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 219..246
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 397..424
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 224
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 226
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 402
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 404
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 409
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 484 AA; 55567 MW; B850B4DEF5D90E27 CRC64;
MTSQFYTNLY EIITILNIPL AIAVIFMERR NVGVTWAWLM VLLFLPVVGF GFYLIFGQNM
SKKKLYKISK RTLSTMNDLI ETQRKEFREH QIVYHDPAME NYQDLIYMNL TSGFALYSQN
NAIDIFTNGN DKFDALIRDI EAATHHIHLM YYIVQPDGLG NRLVDLLTKK ASEGVKVRFL
YDDIGSSHLP RHFFDRLRNA GGEVAAFFPS KIPYLNIRVN YRNHRKLAIM DGTIGYIGGI
NIGDEYLGLN KRFGYWRDSH LRIQGYAVQQ MQAHFMMDWN LASSAAIDRN MEELFPESVD
CGLAGIQIVS SGPDRAMEQI KNAYIKMINA AKESIYIQTP YFIPDESMLN ALKMAALSGV
DVRIMLPSRP DHQMVFWASH SYLGELLAEG IRCYQYDKGF LHAKMIVVDG KVASIGTANF
DIRSFKLNFE INAMIFDSGT AQTLKRVFED DIEDSFELTY DAYMSRPLLQ RFKESCTRLL
SPIL
//
