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Database: UniProt
Entry: U2ZMX6_VIBPR
LinkDB: U2ZMX6_VIBPR
Original site: U2ZMX6_VIBPR 
ID   U2ZMX6_VIBPR            Unreviewed;       484 AA.
AC   U2ZMX6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=cls {ECO:0000313|EMBL:GAD69136.1};
GN   Synonyms=clsA {ECO:0000256|HAMAP-Rule:MF_00190};
GN   ORFNames=VPR01S_23_00480 {ECO:0000313|EMBL:GAD69136.1};
OS   Vibrio proteolyticus NBRC 13287.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD69136.1, ECO:0000313|Proteomes:UP000016570};
RN   [1] {ECO:0000313|EMBL:GAD69136.1, ECO:0000313|Proteomes:UP000016570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD69136.1,
RC   ECO:0000313|Proteomes:UP000016570};
RA   Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA   Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL   Submitted (SEP-2013) 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_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 membrane {ECO:0000256|HAMAP-Rule:MF_00190};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00190}. 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. ClsA sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00190}.
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:GAD69136.1}.
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DR   EMBL; BATJ01000023; GAD69136.1; -; Genomic_DNA.
DR   RefSeq; WP_021707104.1; NZ_BATJ01000023.1.
DR   AlphaFoldDB; U2ZMX6; -.
DR   STRING; 1219065.VPR01S_23_00480; -.
DR   eggNOG; COG1502; Bacteria.
DR   Proteomes; UP000016570; 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; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000016570};
KW   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;  55472 MW;  20B2C706E69333ED CRC64;
     MDKFYHFLTL ASIGLYWLLV AGVTLRVVFK RRAVSVSLAW LMIIYIVPVV GVACYFLFGE
     LNLGRKRADR AKEMFTPFAN WFSQLNECHA HTPERMGRHI YRIDELCNNR LGLPALSGNT
     LSLQSSPHDI LHSIIEDIEQ AQSSIRMVFY IWHPGGLADS VASALIRAAK RGVDVKLLLD
     SAGSPRFFRS SWLKMMKNAG IEVIQALEVS PWRIFLRRLD LRQHRKIIVI DDNIAYTGSM
     NMVDPAYFKQ NAGVGQWIDI MVRVTGPTVN VLSAIHCWDW EVETGARMLP ANPECKLDPN
     QPHHPVQVVP SGPGMPDYLI SQVLTLAINQ ANESVRITTP YFVPSADLLE TLKMTAQRGI
     NVELIIPHKN DSMMVQWASR AFYTELLEAG VKIYEFYGGL LHTKSVVIDK QFCLVGTVNI
     DMRSLWLNFE VTLAIDDEAF TKEMHWLQES YIEQSHFVEL KKWEQRGMYY RFLERLFYLF
     NPLL
//
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