CLSA_PSESM
ID CLSA_PSESM Reviewed; 479 AA.
AC Q87TY7;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=PSPTO_5530;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO58949.1; -; Genomic_DNA.
DR RefSeq; NP_795254.1; NC_004578.1.
DR RefSeq; WP_005768306.1; NC_004578.1.
DR AlphaFoldDB; Q87TY7; -.
DR SMR; Q87TY7; -.
DR STRING; 223283.PSPTO_5530; -.
DR DNASU; 1187222; -.
DR EnsemblBacteria; AAO58949; AAO58949; PSPTO_5530.
DR GeneID; 1187222; -.
DR KEGG; pst:PSPTO_5530; -.
DR PATRIC; fig|223283.9.peg.5666; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_0_6; -.
DR OMA; TRFILDW; -.
DR OrthoDB; 1881748at2; -.
DR PhylomeDB; Q87TY7; -.
DR Proteomes; UP000002515; 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; ISS:JCVI.
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_0000201263"
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; 53565 MW; D715C0550169DB56 CRC64;
MDYHDPYFFG YVLGFIHLLG TGAAIHALLT VRTSQGAIAW AMPLLFIPYF TLLPYLIFGR
SSFDAYIKAR REANKEMRAA IGSLNWRPWI EEAVAARRSD AYAALRAMPR LGNMPALANN
KVRLLINGEE TFGAIFQAIR EAKQTILIQF FIIHDDNLGR QLQTLLLEKA AQGVAIFVLY
DRIGSHALPG AYIDTLRDGG VQIKAFATRG GWLNRFQINF RNHRKIVVVD GLKGYIGGHN
VGDEYMGLKP PLAPWRDTHV EVIGPVVACL QESFAEDWFW ATRELPPLSL PDEFPEDGVL
CQLLTSGPAD AQETCSLFFV EAIHAAEERV WITSPYFIPD EAVSAALTLA VLRGVDVRLL
LPSRPDHYVV YAASSLYAFD AVRAGVRVFR YEPGFLHQKV VLVDNDITAI GSANLDNRSF
RLNFELMLLT VDSDFSSQVE AMLTADFAAA REISLQESHE TRRLHQLGMR VARLISPIL
