ID C9MUE5_9FUSO Unreviewed; 536 AA.
AC C9MUE5;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=GCWU000323_00164 {ECO:0000313|EMBL:EEX75565.1};
OS Leptotrichia hofstadii F0254.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX75565.1, ECO:0000313|Proteomes:UP000006233};
RN [1] {ECO:0000313|EMBL:EEX75565.1, ECO:0000313|Proteomes:UP000006233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0254 {ECO:0000313|EMBL:EEX75565.1,
RC ECO:0000313|Proteomes:UP000006233};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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: 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:EEX75565.1}.
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DR EMBL; ACVB02000006; EEX75565.1; -; Genomic_DNA.
DR RefSeq; WP_006803500.1; NZ_GG700632.1.
DR AlphaFoldDB; C9MUE5; -.
DR STRING; 634994.GCWU000323_00164; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_2_0; -.
DR Proteomes; UP000006233; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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}; Hydrolase {ECO:0000313|EMBL:EEX75565.1};
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:UP000006233};
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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 40..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 261..288
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 449..476
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 266
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 268
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 273
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 454
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 456
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 461
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 536 AA; 62460 MW; 520B716B0D871084 CRC64;
MLHGLAIIIS SWIIPFERLH YLIIIVLTVS VLLSDKSPNA MLAWIFTIFT FPLGGAVLYL
LFGINWRRNK VISKKMKGEE KKLYSRIFNF MQRDVSDIFR SQDFFYYNRL ENVDGNTDKM
TEAEIKATIR NQIDTMIKNI NLGSQQSELV KMLYEAEGTF LTNNDSYKLF FHGKEAFDSI
IFDIENAKST IYMEYFIWKA DELGERIKNA LLKKAKEGVK IKLLFDGVGT WKLPRKYKKE
LRNAGIEIRW FLDVKFFISK MNYRNHRKIA LIDNNIVHTG GMNVGQEYID GGKKFDSWRD
TNIRITGEII GQYLAIFVTD WLNSGGKDDF IEDIKKEAVH ELEEQKPIDK QEKLEYLMQV
SSSGPDTEWT TLKYLYSKMI ATAKEEVLIQ SPYFVPDYDL ISQLKMAALS GVKIKIMVTG
VPDKKMPYWI AETYFAELIG AGIEIYRYTA GFLHSKNIIV DEKISTLGTC NFDMRSFEIN
YEVNSVFYNE NISKDLKEQF IEDLEVCERF DEARLKKVTF MKRLRNSVFK LISPIM
//
