ID Q7MLM7_VIBVY Unreviewed; 484 AA.
AC Q7MLM7;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Cardiolipin synthase A {ECO:0000256|HAMAP-Rule:MF_00190};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_00190};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_00190};
GN Name=clsA {ECO:0000256|HAMAP-Rule:MF_00190};
GN OrderedLocusNames=VV1400 {ECO:0000313|EMBL:BAC94164.1};
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC94164.1, ECO:0000313|Proteomes:UP000002675};
RN [1] {ECO:0000313|EMBL:BAC94164.1, ECO:0000313|Proteomes:UP000002675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016 {ECO:0000313|EMBL:BAC94164.1,
RC ECO:0000313|Proteomes:UP000002675};
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA Tsai S.F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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_00190}.
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_00190};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00190}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00190}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsA sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00190}.
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DR EMBL; BA000037; BAC94164.1; -; Genomic_DNA.
DR RefSeq; WP_011150060.1; NC_005139.1.
DR AlphaFoldDB; Q7MLM7; -.
DR STRING; 672.VV93_v1c13110; -.
DR KEGG; vvy:VV1400; -.
DR PATRIC; fig|196600.6.peg.1388; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_0_6; -.
DR Proteomes; UP000002675; Chromosome I.
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; cd09152; PLDc_EcCLS_like_1; 1.
DR CDD; cd09158; PLDc_EcCLS_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR HAMAP; MF_00190; Cardiolipin_synth_ClsA; 1.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR030840; CL_synthase_A.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_00190};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00190};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00190};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00190}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00190};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00190}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
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_00190"
FT ACT_SITE 226
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 402
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 404
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
FT ACT_SITE 409
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00190"
SQ SEQUENCE 484 AA; 55297 MW; C2EE2536940591C1 CRC64;
MDKFYHFLTL AGIGLYWVLI AGVTFRVVLK RRAVSVSLAW LMIIYILPVL GVACYFLFGE
LNLGRKRAER AKEMFAPFAT WFSQLNDCQA HAPESMGRHI YRIDELCNTR LGLPALSGNT
LSLQRSPEEI LHSVIQDIEN AQSSIRMVFY IWHPGGLADS VASALIQAAK RGVDVKLLLD
SAGSPRFFRS HWHQMMVNAG IHVVQALEVS PWRIFLRRLD LRQHRKIIVI DDEIAYTGSM
NLVDPAYFKQ SSGVGQWVDI MVRLTGPTVN VLSAIHCWDW EVETGHRQLP RLPECPLDST
QYQNPIQVVP SGPGMPENLI SQVLILAINQ ANHSVTITTP YFVPSINLLD TLKMTAQRGI
DVQLIIPHKN DSLMVQWASR SFYSELMEAG VKIFEFYGGL LHTKSVVIDQ EFCLVGTVNI
DMRSLWLNFE LTLAVDDEQF TQQMHQLQQN YKSRAHPVHL SEWNKRSLYS RFLERLYYLF
NPLL
//
