CLS_CLOP1
ID CLS_CLOP1 Reviewed; 476 AA.
AC Q0TQG9; Q9ZNC6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Cardiolipin synthase {ECO:0000255|HAMAP-Rule:MF_01916};
DE Short=CL synthase {ECO:0000255|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN Name=cls; Synonyms=clsD; OrderedLocusNames=CPF_1683;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10585141; DOI=10.1111/j.1348-0421.1999.tb03355.x;
RA Koyama M., Katayama S., Kaji M., Taniguchi Y., Matsushita O., Minami J.,
RA Morita S., Okabe A.;
RT "A Clostridium perfringens hem gene cluster contains a cysG(B) homologue
RT that is involved in cobalamin biosynthesis.";
RL Microbiol. Immunol. 43:947-957(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01916};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01916};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01916}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01916}.
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DR EMBL; AB017186; BAA74786.1; -; Genomic_DNA.
DR EMBL; CP000246; ABG84511.1; -; Genomic_DNA.
DR PIR; T43863; T43863.
DR RefSeq; WP_003454642.1; NC_008261.1.
DR AlphaFoldDB; Q0TQG9; -.
DR SMR; Q0TQG9; -.
DR STRING; 195103.CPF_1683; -.
DR EnsemblBacteria; ABG84511; ABG84511; CPF_1683.
DR GeneID; 29571214; -.
DR KEGG; cpf:CPF_1683; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_1_9; -.
DR OMA; YVHVEFY; -.
DR OrthoDB; 1881748at2; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR TIGRFAMs; TIGR04265; bac_cardiolipin; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..476
FT /note="Cardiolipin synthase"
FT /id="PRO_0000273583"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 207..234
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT DOMAIN 389..416
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 212
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 214
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 219
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 394
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 396
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT ACT_SITE 401
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ SEQUENCE 476 AA; 55052 MW; 17C32FC113F0A9DA CRC64;
MHLFINMIFL INIVFIISII FIERRNPQTT WAWILILTFL PILGFIIYIL FGQNITREKN
FKRKILDDKT KQKYLNSFKS HYKLDNISLK YKDLIMMNFN NDNSTYTQRN DIDLYFDANS
LFEEMIDEIN KAEKFIHMEF YIFKSDEIGK KILQALTKKA KEGVEVKLLV DSIGNSIHKK
DIDKLKAAGG DFKIFFPGFC KYINLRINYR NHRKILIIDS KVAFLGGFNI GDEYLGKDKN
IGHWRDTHTK IKGLAINDLE GRFLLDWSYA NESDLDIDLK KYFINPHSTD LPKKIIGAQI
VSSGPDHTEQ QIKNGYFKII NSAKKNLFIQ TPYFVPDEPM LEALRLAALS GVDVKIMLPG
NPDHKFMGWI ANSYFESLLN AGAKIYLYEK GFLHAKTIVA DSSICSVGTA NMDIRSFSLN
FESNIFIYNE AISKSMEEQF FKDLKVCTKV TLESFEKRSI ISRIGESIIR LVSPLM
