ID B1YJB8_EXIS2 Unreviewed; 503 AA.
AC B1YJB8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
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 OrderedLocusNames=Exig_2047 {ECO:0000313|EMBL:ACB61499.1};
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543 {ECO:0000313|EMBL:ACB61499.1, ECO:0000313|Proteomes:UP000001681};
RN [1] {ECO:0000313|EMBL:ACB61499.1, ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RX PubMed=16489412; DOI=10.1007/s00792-005-0497-5;
RA Rodrigues D.F., Goris J., Vishnivetskaya T., Gilichinsky D.,
RA Thomashow M.F., Tiedje J.M.;
RT "Characterization of Exiguobacterium isolates from the Siberian permafrost.
RT Description of Exiguobacterium sibiricum sp. nov.";
RL Extremophiles 10:285-294(2006).
RN [2] {ECO:0000313|EMBL:ACB61499.1, ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RX PubMed=19019206; DOI=10.1186/1471-2164-9-547;
RA Rodrigues D.F., Ivanova N., He Z., Huebner M., Zhou J., Tiedje J.M.;
RT "Architecture of thermal adaptation in an Exiguobacterium sibiricum strain
RT isolated from 3 million year old permafrost: a genome and transcriptome
RT approach.";
RL BMC Genomics 9:547-547(2008).
RN [3] {ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) 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}.
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DR EMBL; CP001022; ACB61499.1; -; Genomic_DNA.
DR RefSeq; WP_012370917.1; NC_010556.1.
DR AlphaFoldDB; B1YJB8; -.
DR STRING; 262543.Exig_2047; -.
DR KEGG; esi:Exig_2047; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_2_9; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000001681; Chromosome.
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:UP000001681};
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..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 238..265
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 416..443
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 243
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 245
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 250
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 423
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 503 AA; 58118 MW; 691C85B79A450E06 CRC64;
MLRRVQLLMT LLLTVSLIGF LSYYWSVYMV GWLSIVIILV VLSVFVIILL ENRNPERTLV
WALVMMALPV VGVFVYFTFG QNYRRKKMFR LKAMLDEESY IKYRTQFDHG IHNQVFQHGH
YTKVVKLIDS ISRLPISYNS HTKVLTNGQE KFPLLLAEIR QAEHHIHLEY YIVRDDELAL
ELQEALIERA KAGVEIRFLY DAVGCFSTDK SYFKKMELAG IEVRPFFPVV LPFISSKSNY
RNHRKIVVID GTVAFTGGIN VGDEYMGKDK MFGFWRDTHL LVRGEAVSEL QLIFLQDWYY
MTGERLFTPY YMKPLEVMEE STGGVQIIAS GPDEPHETMK SLYFGLITEA RSSVYIASPY
LIPDEDLMTA LKTAAMSGID VRILLPSFPD HKVVFYASRS YFDDLLLAGV KIYEYNKGFM
HSKVIVVDDA IATIGTANMD LRSFHLNFEV NAFLYGTNSV HELTRDFYED FSNSSQVERQ
VFIQRSFGQR LIESISRLFS PLL
//
