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Database: UniProt
Entry: I8UG31_9BACI
LinkDB: I8UG31_9BACI
Original site: I8UG31_9BACI 
ID   I8UG31_9BACI            Unreviewed;       500 AA.
AC   I8UG31;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=A374_08134 {ECO:0000313|EMBL:EIT85788.1};
OS   Fictibacillus macauensis ZFHKF-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT85788.1, ECO:0000313|Proteomes:UP000004080};
RN   [1] {ECO:0000313|EMBL:EIT85788.1, ECO:0000313|Proteomes:UP000004080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT85788.1,
RC   ECO:0000313|Proteomes:UP000004080};
RX   PubMed=22887677; DOI=10.1128/JB.01049-12;
RA   Cai L., Zhang T.;
RT   "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL   J. Bacteriol. 194:4780-4780(2012).
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:EIT85788.1}.
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DR   EMBL; AKKV01000024; EIT85788.1; -; Genomic_DNA.
DR   AlphaFoldDB; I8UG31; -.
DR   STRING; 1196324.A374_08134; -.
DR   PATRIC; fig|1196324.3.peg.1669; -.
DR   eggNOG; COG1502; Bacteria.
DR   Proteomes; UP000004080; 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:SF20; CARDIOLIPIN SYNTHASE YWIE-RELATED; 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:UP000004080};
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        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   TRANSMEM        31..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   TRANSMEM        60..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   DOMAIN          236..263
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          413..440
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   500 AA;  57562 MW;  D96C03C634CE607B CRC64;
     MRRLLEFCFL FLLLACLIVI CFTSLSYGWK WSAASVYVAI IVWTLYSLML ENRTSHFTLV
     WMYVLIFLPF IGYLFYLYSG QLYLKGQLFQ TKLKHDRKEL QLLAEKGTEP NYEALSETGA
     CFAKSSQQLY MTMYHEHTHT DILVNGEETF TALKEKLLAA TSYIHMEYYT FRSDELGRSI
     IDVLIQKAQE GIDVRFLFDG MGSLTFANRD IKRLKTAGVK VYPFLPIKHG FFNQKFNFRN
     HRKIAIIDGK YGFTGGLNIG MEYLGANKKL GFWRDTHLLL QGEAVQALHA IFLLDWNYVT
     NESLMQEHRY TESYSVAGNG SVQVVPSGPD TGQGVMSDLY YSMISCAKQS IWIATPYFVP
     NEAIRTALRV AARKGIQVRV MVPENSDSFL TKYASRSYVP ELLRAGIEIY FYKKGFMHQK
     VVLIDGELAS VGSANMDLRS FHLNFEVNVF LTGHQVVSEL HELYKMDIQD CEHISLKDFK
     ERGRWERSKE SFARLFSGVL
//
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