CLSA_PSEAE
ID CLSA_PSEAE Reviewed; 490 AA.
AC Q9HTH0;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=PA5394;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG08779.1; -; Genomic_DNA.
DR PIR; B82971; B82971.
DR RefSeq; NP_254081.1; NC_002516.2.
DR RefSeq; WP_003121332.1; NZ_QZGE01000031.1.
DR AlphaFoldDB; Q9HTH0; -.
DR SMR; Q9HTH0; -.
DR STRING; 287.DR97_2770; -.
DR PaxDb; Q9HTH0; -.
DR EnsemblBacteria; AAG08779; AAG08779; PA5394.
DR GeneID; 883132; -.
DR KEGG; pae:PA5394; -.
DR PATRIC; fig|208964.12.peg.5654; -.
DR PseudoCAP; PA5394; -.
DR HOGENOM; CLU_038053_1_0_6; -.
DR InParanoid; Q9HTH0; -.
DR OMA; TRFILDW; -.
DR PhylomeDB; Q9HTH0; -.
DR BioCyc; PAER208964:G1FZ6-5521-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
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; 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..490
FT /note="Cardiolipin synthase A"
FT /id="PRO_0000201260"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 229..256
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT DOMAIN 403..430
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 234
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 236
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 241
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 408
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 410
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT ACT_SITE 415
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ SEQUENCE 490 AA; 54558 MW; 9195298D93F38EEC CRC64;
MAATGVDKDR PRAMTSTTYL GLLLVGIQVL GFVAAIHAVL TVRTAQGAIA WATSLVFMPY
LTLLPYLVFG RSRFDAYIEA RRQANREMHL AAAELDWRPW VEEALAARQV SGYKGLKALV
RMTRTPTLAN NRVRLLVNGE ASFEAMFKAI SAARQVILVQ FFIVRDDALG QRLQQLLLER
AANGVEVFFL YDAIGSHALP HRYVERLRQG GVQMHGFSTG SGMLNRFQVN FRNHRKVVVV
DGECGFVGGH NVGVEYLGEK PPLAPWRDTH MELRGPAVAC LQESFAEDWY WATHSLPPLI
LPPQYDSEGA LCQVVASGPA DAQETCSLFF VEMINAAHER VWITSPYFVP DEAVMAALRL
AVLRGVDVRL LIPSRPDHRT VYAASSLYAL EAIRAGVKVF RYQPGFLHQK VVLVDRDTAA
VGSANLDNRS FRLNFEVMVV TVDEGFAGEV EAMLEADFAE SLEFTPEDRR SVRRLQQLGM
RVARLVSPIL
