CLSA_PSEPK
ID CLSA_PSEPK Reviewed; 481 AA.
AC Q88C19;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=PP_5364;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN70929.1; -; Genomic_DNA.
DR RefSeq; NP_747465.1; NC_002947.4.
DR AlphaFoldDB; Q88C19; -.
DR SMR; Q88C19; -.
DR STRING; 160488.PP_5364; -.
DR EnsemblBacteria; AAN70929; AAN70929; PP_5364.
DR KEGG; ppu:PP_5364; -.
DR PATRIC; fig|160488.4.peg.5719; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_0_6; -.
DR OMA; HASRSYF; -.
DR PhylomeDB; Q88C19; -.
DR BioCyc; PPUT160488:G1G01-5720-MON; -.
DR Proteomes; UP000000556; 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; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13091; PLDc_2; 2.
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..481
FT /note="Cardiolipin synthase A"
FT /id="PRO_0000201262"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 220..247
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 394..421
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 225
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 227
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 232
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 399
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 401
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 406
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ SEQUENCE 481 AA; 54374 MW; D30AC0AF4DEB4D4B CRC64;
MHMDYHSPYF FGYLLGLIHL LGIVAALHAL FTVRTAQGAI AWAMPLLFIP YLTLIPYLIF
GARSFYAYIK ARRQANQEMH VAMANLNWRP WVEEALTARE SESYTALRAM PKLGRMPCLA
NNQVKLLING KATFDAIFAA IEKARDVVLV QFFIIHDDTL GKALQQLLLR KAAEGVQVFV
LYDRVGSHAL PSSYSQVLRD GGVQIHAFAT RRGWFNRFQV NFRNHRKIVV VDGLLGFIGG
HNVGDEYLGE HPQLSPWRDT HVQISGPVLA CLQESFAEDW YWATRQLPPL ILPDTYPDNG
VLCQALASGP ADPQETCSLF FLEAIHSATR RVWITSPYFI PDEAVFAALR LAVLRGVDVR
VLIPSRPDHR IVYAASSLFA FEAVRAGVRM FRYQPGFLHQ KVVLVDDDVS AIGSANLDNR
SFRLNFEITL LTVDRGFADQ VEHMLQEDFE QAREITAEDT QDTHRLQQLG MRIARLISPI
L
