CLSA_EDWI9
ID CLSA_EDWI9 Reviewed; 486 AA.
AC C5BDA3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Cardiolipin synthase A {ECO:0000255|HAMAP-Rule:MF_00190};
DE Short=CL synthase {ECO:0000255|HAMAP-Rule:MF_00190};
DE EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_00190};
GN Name=clsA {ECO:0000255|HAMAP-Rule:MF_00190}; Synonyms=cls;
GN OrderedLocusNames=NT01EI_1674;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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:0000255|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:0000255|HAMAP-
CC Rule:MF_00190};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00190}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00190}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsA sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_00190}.
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DR EMBL; CP001600; ACR68855.1; -; Genomic_DNA.
DR RefSeq; WP_015871011.1; NC_012779.2.
DR AlphaFoldDB; C5BDA3; -.
DR SMR; C5BDA3; -.
DR STRING; 67780.B6E78_01555; -.
DR EnsemblBacteria; ACR68855; ACR68855; NT01EI_1674.
DR GeneID; 7958907; -.
DR KEGG; eic:NT01EI_1674; -.
DR PATRIC; fig|634503.3.peg.1500; -.
DR HOGENOM; CLU_038053_1_0_6; -.
DR OMA; TRFILDW; -.
DR OrthoDB; 1881748at2; -.
DR Proteomes; UP000001485; 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_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 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 inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..486
FT /note="Cardiolipin synthase A"
FT /id="PRO_1000203994"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 219..246
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 399..426
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 224
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 226
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 231
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 404
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 406
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 411
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ SEQUENCE 486 AA; 54966 MW; AEC40B754C68430A CRC64;
MSTFYTVISW LAIFGYWLLI ASVTLRILMK RRAVPSAMAW LLIIYILPLV GIIAYLSFGE
LHLGKRRAER ARTMWPSTAR WLADLRSCRS IFATHNSEVA APLFQLCERR QGIAGVKGNQ
LQLLTSTDDT LNALIRDIEL AHTSIEMMFY IWQPGGLADR VAEAMMAAAR RGIRCRLMLD
SAGSVAFFRS PYPAMMREAG IEVVEALQVN LLRVFLRRMD LRQHRKVVLI DNFIAYTGSM
NLVDPRYFKQ DAGVGQWIDV MARMEGPVAT TMGIYYAFDW EMETGKRILP PEPICNILPF
EKESGHTIQV IASGPGFPEE LIHQSLLTAV YSARQQLVMT TPYFVPSDDL LHAICTAAQR
GVDVSIIVPK KNDSMMVGWA SRAFFTEMLA AGVKIYQFEG GLLHTKSVLV DGQLSLVGTV
NLDMRSLWLN FEITLVIDDD GFGSDLACVQ EDYIARSSLL DPLEWLKRPL WQRVVERLFY
FFSPLL