ID A0A069CZH3_WEIOS Unreviewed; 478 AA.
AC A0A069CZH3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:GAK30491.1};
GN ORFNames=WOSG25_030880 {ECO:0000313|EMBL:GAK30491.1};
OS Weissella oryzae (strain DSM 25784 / JCM 18191 / LMG 30913 / SG25).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; Weissella.
OX NCBI_TaxID=1329250 {ECO:0000313|EMBL:GAK30491.1, ECO:0000313|Proteomes:UP000030643};
RN [1] {ECO:0000313|Proteomes:UP000030643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25784 / JCM 18191 / LMG 30913 / SG25
RC {ECO:0000313|Proteomes:UP000030643};
RX PubMed=25013139; DOI=10.1128/genomea.00667-14;
RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Suzuki Y.,
RA Nakamura Y., Tohno M.;
RT "Draft genome sequence of Weissella oryzae SG25T, isolated from fermented
RT rice grains.";
RL Genome Announc. 2:0-0(2014).
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; DF820486; GAK30491.1; -; Genomic_DNA.
DR RefSeq; WP_027698595.1; NZ_DF820486.1.
DR AlphaFoldDB; A0A069CZH3; -.
DR STRING; 1329250.WOSG25_030880; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000030643; 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:UP000030643};
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 35..56
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 391..418
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 396
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 398
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 403
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 478 AA; 54572 MW; 87A491C75FC0A3B3 CRC64;
MASNVILRTV ELIVLLNIIA AVITVFREKR DISSIWAWLL VLIFFPVVGF MIYFILGRKL
SNKHIFNLQA QEAMGIDRIA EHQAALLSAN DGRSEAEAFI RLFLKNDEAI FTQANAVKIF
DDGYEKFTAL LFDIANAKHH INVEYFTIYD DEIGNQIINA LTQSAARGVR VRVIYDMWGS
HGRHKRLFKP LKDAGGQVEA FLMPWWQPFT FRINNRMHRK LVIIDGNIGY VGGFNIGDQY
VGKFKKFGYW RDTHLRIAGD AVLAMQSRFF LDWNATTRKA KIDFADEYFP SPVVQGNVAM
QIVSSGPDSE VKQIYQGYLQ LFARAKESIT IQTPYFIPKQ AMLELLQLAA MAGVKVRLMI
PNRPDHVFVY RATQYFAREL MLAGGEVYTY EGGFLHAKVV VVDGKFASVG TANMDIRSFD
LNFEVNAFMY DQTIAQDLEA QFENDLKQAK RVTEATYAAQ SHWLTFKQMF SRLLAPIL
//
