CLSA_PSEFS
ID CLSA_PSEFS Reviewed; 479 AA.
AC C3K1C4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=PFLU_6096;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(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; AM181176; CAY53688.1; -; Genomic_DNA.
DR RefSeq; WP_015886623.1; NC_012660.1.
DR AlphaFoldDB; C3K1C4; -.
DR SMR; C3K1C4; -.
DR STRING; 216595.PFLU_6096; -.
DR EnsemblBacteria; CAY53688; CAY53688; PFLU_6096.
DR KEGG; pfs:PFLU_6096; -.
DR PATRIC; fig|216595.4.peg.6220; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_0_6; -.
DR OMA; TRFILDW; -.
DR OrthoDB; 1881748at2; -.
DR Proteomes; UP000002332; 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..479
FT /note="Cardiolipin synthase A"
FT /id="PRO_1000203998"
FT TRANSMEM 8..28
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 218..245
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 392..419
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 223
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 225
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 230
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 397
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 399
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 404
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ SEQUENCE 479 AA; 53772 MW; DF58A66CB1F7E39E CRC64;
MDFFGPHLLA YFIATLHFLG TLAAIHAVLT VRTAQGSIAW ALSLMFMPYL TLIPYLIFGR
STFDAYIQAR RQANQEMHTA ITALNWRPWV EEALAARNSS AYASLRAMPK LGRMPCLANN
EVHLLINGDA TFSAIFEAIR NARTAVLFQF FIIHDDELGR QLHALLKEKS AEGVAIYVLY
DRIGSHALPH RYVQSLRDAG VQVKAFATRS GWLNRFQVNF RNHRKIVVVD GITGFVGGHN
VGDEYLGKKP PLAPWRDTHV QVTGPVVACL QESFAEDWFW AARELPPLIL PDAYPEDGVL
CQLLASGPAD PYETCSLFFV EAIHAATERV WITSPYFIPD EAVFAALRLA VLRGVDVRLL
LPSRPDHRIV YAASSLYAIE AVRAGVRVFR YTPGFLHQKV VLVDSEISAI GSANMDNRSF
RLNFEVMLLT VDEAFAKEVE HMLLDDFALA HEVSQEESRE TRRLQQLGMR VARLISPIL
