CLSA_ESCF3
ID CLSA_ESCF3 Reviewed; 486 AA.
AC B7LS29;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=EFER_1705;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ89221.1; -; Genomic_DNA.
DR RefSeq; WP_000206880.1; NC_011740.1.
DR AlphaFoldDB; B7LS29; -.
DR SMR; B7LS29; -.
DR EnsemblBacteria; CAQ89221; CAQ89221; EFER_1705.
DR GeneID; 60900497; -.
DR KEGG; efe:EFER_1705; -.
DR HOGENOM; CLU_038053_1_0_6; -.
DR OMA; TRFILDW; -.
DR OrthoDB; 1881748at2; -.
DR BioCyc; EFER585054:EFER_RS08570-MON; -.
DR Proteomes; UP000000745; 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; Repeat;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..486
FT /note="Cardiolipin synthase A"
FT /id="PRO_1000118591"
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; 54902 MW; F440C07FCD9889BE CRC64;
MTTFYTVVSW LVILGYWLLI AGVTLRILMK RRAVPSAMAW LLIIYILPLV GIIAYLSFGE
LHLGKRRAER ARAMWPSTAK WLNDLKSCKH IFAEENSSVA SSLFKLCERR QGIAGVKGNQ
LQLLTDSDDV MQALIRDIQL ARHNIEMVFY IWQPGGMADK VAESLMAAAR RGIHCRLMLD
SAGSVAFFRS PWAAMMRNAG IEVVEALKVN LMRVFLRRMD LRQHRKMIMI DNYIAYTGSM
NMVDPRFFKQ DAGVGQWVDV MARMEGPIAT AMGVIYSCDW EIETGKRILP PPPDVNIMPF
EQASGHTIHT IASGPGFPED LIHQALLTAT YSAREYLIMT TPYFVPSDDL LHAICTAAQR
GVDVSIILPR KNDSMLVGWA SRAFFTELLA AGVKIYQFEG GLLHTKSVLV DGELSLVGTV
NLDMRSLWLN FEITLAIDDK GFGADLAAVQ DDYISRSRLL DERLWLKRPL WQRVAERLFY
FFSPLL
